Crystallographic Trapping of the Glutamyl-CoA Thioester Intermediate of Family I CoA Transferases

Coenzyme A transferases are involved in a broad range of biochemical processes in both prokaryotes and eukaryotes, and exhibit a diverse range of substrate specificities. The YdiF protein from Escherichia coli O157:H7 is an acyl-CoA transferase of unknown physiological function, and belongs to a lar...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:The Journal of biological chemistry 2005-12, Vol.280 (52), p.42919-42928
Hauptverfasser: Rangarajan, Erumbi S., Li, Yunge, Ajamian, Eunice, Iannuzzi, Pietro, Kernaghan, Stephanie D., Fraser, Marie E., Cygler, Miroslaw, Matte, Allan
Format: Artikel
Sprache:eng
Schlagworte:
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
container_end_page 42928
container_issue 52
container_start_page 42919
container_title The Journal of biological chemistry
container_volume 280
creator Rangarajan, Erumbi S.
Li, Yunge
Ajamian, Eunice
Iannuzzi, Pietro
Kernaghan, Stephanie D.
Fraser, Marie E.
Cygler, Miroslaw
Matte, Allan
description Coenzyme A transferases are involved in a broad range of biochemical processes in both prokaryotes and eukaryotes, and exhibit a diverse range of substrate specificities. The YdiF protein from Escherichia coli O157:H7 is an acyl-CoA transferase of unknown physiological function, and belongs to a large sequence family of CoA transferases, present in bacteria to humans, which utilize oxoacids as acceptors. In vitro measurements showed that YdiF displays enzymatic activity with short-chain acyl-CoAs. The crystal structures of YdiF and its complex with CoA, the first co-crystal structure for any Family I CoA transferase, have been determined and refined at 1.9 and 2.0 Å resolution, respectively. YdiF is organized into tetramers, with each monomer having an open α/β structure characteristic of Family I CoA transferases. Co-crystallization of YdiF with a variety of CoA thioesters in the absence of acceptor carboxylic acid resulted in trapping a covalent γ-glutamyl-CoA thioester intermediate. The CoA binds within a well defined pocket at the N- and C-terminal domain interface, but makes contact only with the C-terminal domain. The structure of the YdiF complex provides a basis for understanding the different catalytic steps in the reaction of Family I CoA transferases.
doi_str_mv 10.1074/jbc.M510522200
format Article
fullrecord <record><control><sourceid>proquest_osti_</sourceid><recordid>TN_cdi_osti_scitechconnect_913922</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S0021925819479015</els_id><sourcerecordid>68921400</sourcerecordid><originalsourceid>FETCH-LOGICAL-c5130-86d3014c863fe593f09105f108243362a70e375fb42f6199af2bd837653beb523</originalsourceid><addsrcrecordid>eNqFkTFv2zAQhYmiReOkXTsWKhBkk3MkRZkcAyNJDaTo4gDdCIo-Wgwk0SXlFv73pSoDmYrewFs-vrt3j5BPFJYUVtXtS2OX3wQFwRgDeEMWFCQvuaA_3pIFAKOlYkJekMuUXiBXpeh7ckFrJriSckHMOp7SaLou7KM5tN4W29wPftgXwRVji8VjdxxNf-rKdbgrtq0PmEaMxWbIb487b0ac0AfT--5UbIq_WDRDchhNwvSBvHOmS_jx3K_I88P9dv21fPr-uFnfPZVWUA6lrHccaGVlzR0KxR2o7MplO6zivGZmBchXwjUVczVVyjjW7CRf1YI32AjGr8iXWTek0etk_Yi2tWEY0I5aUa7YxNzMzCGGn8dsRPc-Wew6M2A4Jl1LxWgF8F-Qqjy4kpPicgZtDClFdPoQfW_iSVPQU0I6J6RfE8ofPp-Vj00-3yt-jiQD1zPQ-n3720fUjQ-2xV4zCVowXTFFVcbkjGG-6S-PcbKMg82JxMnxLvh_rfAHwmeowQ</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>19765482</pqid></control><display><type>article</type><title>Crystallographic Trapping of the Glutamyl-CoA Thioester Intermediate of Family I CoA Transferases</title><source>MEDLINE</source><source>EZB-FREE-00999 freely available EZB journals</source><source>PubMed Central</source><source>Alma/SFX Local Collection</source><creator>Rangarajan, Erumbi S. ; Li, Yunge ; Ajamian, Eunice ; Iannuzzi, Pietro ; Kernaghan, Stephanie D. ; Fraser, Marie E. ; Cygler, Miroslaw ; Matte, Allan</creator><creatorcontrib>Rangarajan, Erumbi S. ; Li, Yunge ; Ajamian, Eunice ; Iannuzzi, Pietro ; Kernaghan, Stephanie D. ; Fraser, Marie E. ; Cygler, Miroslaw ; Matte, Allan ; Brookhaven National Laboratory (BNL) National Synchrotron Light Source</creatorcontrib><description>Coenzyme A transferases are involved in a broad range of biochemical processes in both prokaryotes and eukaryotes, and exhibit a diverse range of substrate specificities. The YdiF protein from Escherichia coli O157:H7 is an acyl-CoA transferase of unknown physiological function, and belongs to a large sequence family of CoA transferases, present in bacteria to humans, which utilize oxoacids as acceptors. In vitro measurements showed that YdiF displays enzymatic activity with short-chain acyl-CoAs. The crystal structures of YdiF and its complex with CoA, the first co-crystal structure for any Family I CoA transferase, have been determined and refined at 1.9 and 2.0 Å resolution, respectively. YdiF is organized into tetramers, with each monomer having an open α/β structure characteristic of Family I CoA transferases. Co-crystallization of YdiF with a variety of CoA thioesters in the absence of acceptor carboxylic acid resulted in trapping a covalent γ-glutamyl-CoA thioester intermediate. The CoA binds within a well defined pocket at the N- and C-terminal domain interface, but makes contact only with the C-terminal domain. The structure of the YdiF complex provides a basis for understanding the different catalytic steps in the reaction of Family I CoA transferases.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1074/jbc.M510522200</identifier><identifier>PMID: 16253988</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>BACTERIA ; Binding Sites ; CARBOXYLIC ACIDS ; Carboxylic Acids - chemistry ; Catalysis ; Catalytic Domain ; Chromatography, Gel ; Cloning, Molecular ; Coenzyme A - chemistry ; Coenzyme A-Transferases - chemistry ; Coenzyme A-Transferases - metabolism ; COENZYMES ; CRYSTAL STRUCTURE ; Crystallization ; CRYSTALLOGRAPHY ; Crystallography, X-Ray - methods ; ESCHERICHIA COLI ; Escherichia coli - enzymology ; Escherichia coli - metabolism ; Escherichia coli Proteins - chemistry ; Escherichia coli Proteins - metabolism ; Esters - chemistry ; Glutamic Acid - chemistry ; Histidine - chemistry ; IN VITRO ; Mass Spectrometry ; MATERIALS SCIENCE ; Models, Chemical ; Models, Molecular ; Molecular Conformation ; MONOMERS ; national synchrotron light source ; Protein Conformation ; Protein Folding ; Protein Structure, Quaternary ; Protein Structure, Secondary ; Protein Structure, Tertiary ; PROTEINS ; RESOLUTION ; SUBSTRATES ; TRANSFERASES ; TRAPPING</subject><ispartof>The Journal of biological chemistry, 2005-12, Vol.280 (52), p.42919-42928</ispartof><rights>2005 © 2005 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5130-86d3014c863fe593f09105f108243362a70e375fb42f6199af2bd837653beb523</citedby><cites>FETCH-LOGICAL-c5130-86d3014c863fe593f09105f108243362a70e375fb42f6199af2bd837653beb523</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,314,780,784,885,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16253988$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://www.osti.gov/biblio/913922$$D View this record in Osti.gov$$Hfree_for_read</backlink></links><search><creatorcontrib>Rangarajan, Erumbi S.</creatorcontrib><creatorcontrib>Li, Yunge</creatorcontrib><creatorcontrib>Ajamian, Eunice</creatorcontrib><creatorcontrib>Iannuzzi, Pietro</creatorcontrib><creatorcontrib>Kernaghan, Stephanie D.</creatorcontrib><creatorcontrib>Fraser, Marie E.</creatorcontrib><creatorcontrib>Cygler, Miroslaw</creatorcontrib><creatorcontrib>Matte, Allan</creatorcontrib><creatorcontrib>Brookhaven National Laboratory (BNL) National Synchrotron Light Source</creatorcontrib><title>Crystallographic Trapping of the Glutamyl-CoA Thioester Intermediate of Family I CoA Transferases</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>Coenzyme A transferases are involved in a broad range of biochemical processes in both prokaryotes and eukaryotes, and exhibit a diverse range of substrate specificities. The YdiF protein from Escherichia coli O157:H7 is an acyl-CoA transferase of unknown physiological function, and belongs to a large sequence family of CoA transferases, present in bacteria to humans, which utilize oxoacids as acceptors. In vitro measurements showed that YdiF displays enzymatic activity with short-chain acyl-CoAs. The crystal structures of YdiF and its complex with CoA, the first co-crystal structure for any Family I CoA transferase, have been determined and refined at 1.9 and 2.0 Å resolution, respectively. YdiF is organized into tetramers, with each monomer having an open α/β structure characteristic of Family I CoA transferases. Co-crystallization of YdiF with a variety of CoA thioesters in the absence of acceptor carboxylic acid resulted in trapping a covalent γ-glutamyl-CoA thioester intermediate. The CoA binds within a well defined pocket at the N- and C-terminal domain interface, but makes contact only with the C-terminal domain. The structure of the YdiF complex provides a basis for understanding the different catalytic steps in the reaction of Family I CoA transferases.</description><subject>BACTERIA</subject><subject>Binding Sites</subject><subject>CARBOXYLIC ACIDS</subject><subject>Carboxylic Acids - chemistry</subject><subject>Catalysis</subject><subject>Catalytic Domain</subject><subject>Chromatography, Gel</subject><subject>Cloning, Molecular</subject><subject>Coenzyme A - chemistry</subject><subject>Coenzyme A-Transferases - chemistry</subject><subject>Coenzyme A-Transferases - metabolism</subject><subject>COENZYMES</subject><subject>CRYSTAL STRUCTURE</subject><subject>Crystallization</subject><subject>CRYSTALLOGRAPHY</subject><subject>Crystallography, X-Ray - methods</subject><subject>ESCHERICHIA COLI</subject><subject>Escherichia coli - enzymology</subject><subject>Escherichia coli - metabolism</subject><subject>Escherichia coli Proteins - chemistry</subject><subject>Escherichia coli Proteins - metabolism</subject><subject>Esters - chemistry</subject><subject>Glutamic Acid - chemistry</subject><subject>Histidine - chemistry</subject><subject>IN VITRO</subject><subject>Mass Spectrometry</subject><subject>MATERIALS SCIENCE</subject><subject>Models, Chemical</subject><subject>Models, Molecular</subject><subject>Molecular Conformation</subject><subject>MONOMERS</subject><subject>national synchrotron light source</subject><subject>Protein Conformation</subject><subject>Protein Folding</subject><subject>Protein Structure, Quaternary</subject><subject>Protein Structure, Secondary</subject><subject>Protein Structure, Tertiary</subject><subject>PROTEINS</subject><subject>RESOLUTION</subject><subject>SUBSTRATES</subject><subject>TRANSFERASES</subject><subject>TRAPPING</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkTFv2zAQhYmiReOkXTsWKhBkk3MkRZkcAyNJDaTo4gDdCIo-Wgwk0SXlFv73pSoDmYrewFs-vrt3j5BPFJYUVtXtS2OX3wQFwRgDeEMWFCQvuaA_3pIFAKOlYkJekMuUXiBXpeh7ckFrJriSckHMOp7SaLou7KM5tN4W29wPftgXwRVji8VjdxxNf-rKdbgrtq0PmEaMxWbIb487b0ac0AfT--5UbIq_WDRDchhNwvSBvHOmS_jx3K_I88P9dv21fPr-uFnfPZVWUA6lrHccaGVlzR0KxR2o7MplO6zivGZmBchXwjUVczVVyjjW7CRf1YI32AjGr8iXWTek0etk_Yi2tWEY0I5aUa7YxNzMzCGGn8dsRPc-Wew6M2A4Jl1LxWgF8F-Qqjy4kpPicgZtDClFdPoQfW_iSVPQU0I6J6RfE8ofPp-Vj00-3yt-jiQD1zPQ-n3720fUjQ-2xV4zCVowXTFFVcbkjGG-6S-PcbKMg82JxMnxLvh_rfAHwmeowQ</recordid><startdate>20051230</startdate><enddate>20051230</enddate><creator>Rangarajan, Erumbi S.</creator><creator>Li, Yunge</creator><creator>Ajamian, Eunice</creator><creator>Iannuzzi, Pietro</creator><creator>Kernaghan, Stephanie D.</creator><creator>Fraser, Marie E.</creator><creator>Cygler, Miroslaw</creator><creator>Matte, Allan</creator><general>Elsevier Inc</general><general>American Society for Biochemistry and Molecular Biology</general><scope>6I.</scope><scope>AAFTH</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QL</scope><scope>C1K</scope><scope>7X8</scope><scope>OTOTI</scope></search><sort><creationdate>20051230</creationdate><title>Crystallographic Trapping of the Glutamyl-CoA Thioester Intermediate of Family I CoA Transferases</title><author>Rangarajan, Erumbi S. ; Li, Yunge ; Ajamian, Eunice ; Iannuzzi, Pietro ; Kernaghan, Stephanie D. ; Fraser, Marie E. ; Cygler, Miroslaw ; Matte, Allan</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5130-86d3014c863fe593f09105f108243362a70e375fb42f6199af2bd837653beb523</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2005</creationdate><topic>BACTERIA</topic><topic>Binding Sites</topic><topic>CARBOXYLIC ACIDS</topic><topic>Carboxylic Acids - chemistry</topic><topic>Catalysis</topic><topic>Catalytic Domain</topic><topic>Chromatography, Gel</topic><topic>Cloning, Molecular</topic><topic>Coenzyme A - chemistry</topic><topic>Coenzyme A-Transferases - chemistry</topic><topic>Coenzyme A-Transferases - metabolism</topic><topic>COENZYMES</topic><topic>CRYSTAL STRUCTURE</topic><topic>Crystallization</topic><topic>CRYSTALLOGRAPHY</topic><topic>Crystallography, X-Ray - methods</topic><topic>ESCHERICHIA COLI</topic><topic>Escherichia coli - enzymology</topic><topic>Escherichia coli - metabolism</topic><topic>Escherichia coli Proteins - chemistry</topic><topic>Escherichia coli Proteins - metabolism</topic><topic>Esters - chemistry</topic><topic>Glutamic Acid - chemistry</topic><topic>Histidine - chemistry</topic><topic>IN VITRO</topic><topic>Mass Spectrometry</topic><topic>MATERIALS SCIENCE</topic><topic>Models, Chemical</topic><topic>Models, Molecular</topic><topic>Molecular Conformation</topic><topic>MONOMERS</topic><topic>national synchrotron light source</topic><topic>Protein Conformation</topic><topic>Protein Folding</topic><topic>Protein Structure, Quaternary</topic><topic>Protein Structure, Secondary</topic><topic>Protein Structure, Tertiary</topic><topic>PROTEINS</topic><topic>RESOLUTION</topic><topic>SUBSTRATES</topic><topic>TRANSFERASES</topic><topic>TRAPPING</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Rangarajan, Erumbi S.</creatorcontrib><creatorcontrib>Li, Yunge</creatorcontrib><creatorcontrib>Ajamian, Eunice</creatorcontrib><creatorcontrib>Iannuzzi, Pietro</creatorcontrib><creatorcontrib>Kernaghan, Stephanie D.</creatorcontrib><creatorcontrib>Fraser, Marie E.</creatorcontrib><creatorcontrib>Cygler, Miroslaw</creatorcontrib><creatorcontrib>Matte, Allan</creatorcontrib><creatorcontrib>Brookhaven National Laboratory (BNL) National Synchrotron Light Source</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Environmental Sciences and Pollution Management</collection><collection>MEDLINE - Academic</collection><collection>OSTI.GOV</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Rangarajan, Erumbi S.</au><au>Li, Yunge</au><au>Ajamian, Eunice</au><au>Iannuzzi, Pietro</au><au>Kernaghan, Stephanie D.</au><au>Fraser, Marie E.</au><au>Cygler, Miroslaw</au><au>Matte, Allan</au><aucorp>Brookhaven National Laboratory (BNL) National Synchrotron Light Source</aucorp><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Crystallographic Trapping of the Glutamyl-CoA Thioester Intermediate of Family I CoA Transferases</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>2005-12-30</date><risdate>2005</risdate><volume>280</volume><issue>52</issue><spage>42919</spage><epage>42928</epage><pages>42919-42928</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>Coenzyme A transferases are involved in a broad range of biochemical processes in both prokaryotes and eukaryotes, and exhibit a diverse range of substrate specificities. The YdiF protein from Escherichia coli O157:H7 is an acyl-CoA transferase of unknown physiological function, and belongs to a large sequence family of CoA transferases, present in bacteria to humans, which utilize oxoacids as acceptors. In vitro measurements showed that YdiF displays enzymatic activity with short-chain acyl-CoAs. The crystal structures of YdiF and its complex with CoA, the first co-crystal structure for any Family I CoA transferase, have been determined and refined at 1.9 and 2.0 Å resolution, respectively. YdiF is organized into tetramers, with each monomer having an open α/β structure characteristic of Family I CoA transferases. Co-crystallization of YdiF with a variety of CoA thioesters in the absence of acceptor carboxylic acid resulted in trapping a covalent γ-glutamyl-CoA thioester intermediate. The CoA binds within a well defined pocket at the N- and C-terminal domain interface, but makes contact only with the C-terminal domain. The structure of the YdiF complex provides a basis for understanding the different catalytic steps in the reaction of Family I CoA transferases.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>16253988</pmid><doi>10.1074/jbc.M510522200</doi><tpages>10</tpages><oa>free_for_read</oa></addata></record>
fulltext fulltext
identifier ISSN: 0021-9258
ispartof The Journal of biological chemistry, 2005-12, Vol.280 (52), p.42919-42928
issn 0021-9258
1083-351X
language eng
recordid cdi_osti_scitechconnect_913922
source MEDLINE; EZB-FREE-00999 freely available EZB journals; PubMed Central; Alma/SFX Local Collection
subjects BACTERIA
Binding Sites
CARBOXYLIC ACIDS
Carboxylic Acids - chemistry
Catalysis
Catalytic Domain
Chromatography, Gel
Cloning, Molecular
Coenzyme A - chemistry
Coenzyme A-Transferases - chemistry
Coenzyme A-Transferases - metabolism
COENZYMES
CRYSTAL STRUCTURE
Crystallization
CRYSTALLOGRAPHY
Crystallography, X-Ray - methods
ESCHERICHIA COLI
Escherichia coli - enzymology
Escherichia coli - metabolism
Escherichia coli Proteins - chemistry
Escherichia coli Proteins - metabolism
Esters - chemistry
Glutamic Acid - chemistry
Histidine - chemistry
IN VITRO
Mass Spectrometry
MATERIALS SCIENCE
Models, Chemical
Models, Molecular
Molecular Conformation
MONOMERS
national synchrotron light source
Protein Conformation
Protein Folding
Protein Structure, Quaternary
Protein Structure, Secondary
Protein Structure, Tertiary
PROTEINS
RESOLUTION
SUBSTRATES
TRANSFERASES
TRAPPING
title Crystallographic Trapping of the Glutamyl-CoA Thioester Intermediate of Family I CoA Transferases
url https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-23T01%3A28%3A53IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_osti_&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Crystallographic%20Trapping%20of%20the%20Glutamyl-CoA%20Thioester%20Intermediate%20of%20Family%20I%20CoA%20Transferases&rft.jtitle=The%20Journal%20of%20biological%20chemistry&rft.au=Rangarajan,%20Erumbi%20S.&rft.aucorp=Brookhaven%20National%20Laboratory%20(BNL)%20National%20Synchrotron%20Light%20Source&rft.date=2005-12-30&rft.volume=280&rft.issue=52&rft.spage=42919&rft.epage=42928&rft.pages=42919-42928&rft.issn=0021-9258&rft.eissn=1083-351X&rft_id=info:doi/10.1074/jbc.M510522200&rft_dat=%3Cproquest_osti_%3E68921400%3C/proquest_osti_%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=19765482&rft_id=info:pmid/16253988&rft_els_id=S0021925819479015&rfr_iscdi=true