Escherichia coli cyclophilin B binds a highly distorted form of trans‐prolyl peptide isomer

Cyclophilins facilitate the peptidyl‐prolyl isomerization of a trans‐isomer to a cis‐isomer in the refolding process of unfolded proteins to recover the natural folding state with cis‐proline conformation. To date, only short peptides with a cis‐form proline have been observed in complexes of human...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:European journal of biochemistry 2004-09, Vol.271 (18), p.3794-3803
Hauptverfasser: Konno, Michiko, Sano, Yumi, Okudaira, Kayoko, Kawaguchi, Yoko, Yamagishi‐Ohmori, Yoko, Fushinobu, Shinya, Matsuzawa, Hiroshi
Format: Artikel
Sprache:eng
Schlagworte:
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
container_end_page 3803
container_issue 18
container_start_page 3794
container_title European journal of biochemistry
container_volume 271
creator Konno, Michiko
Sano, Yumi
Okudaira, Kayoko
Kawaguchi, Yoko
Yamagishi‐Ohmori, Yoko
Fushinobu, Shinya
Matsuzawa, Hiroshi
description Cyclophilins facilitate the peptidyl‐prolyl isomerization of a trans‐isomer to a cis‐isomer in the refolding process of unfolded proteins to recover the natural folding state with cis‐proline conformation. To date, only short peptides with a cis‐form proline have been observed in complexes of human and Escherichia coli proteins of cyclophilin A, which is present in cytoplasm. The crystal structures analyzed in this study show two complexes in which peptides having a trans‐form proline, i.e. succinyl‐Ala‐trans‐Pro‐Ala‐p‐nitroanilide and acetyl‐Ala‐Ala‐trans‐Pro‐Ala‐amidomethylcoumarin, are bound on a K163T mutant of Escherichia coli cyclophilin B, the preprotein of which has a signal sequence. Comparison with cis‐form peptides bound to cyclophilin A reveals that in any case the proline ring is inserted into the hydrophobic pocket and a hydrogen bond between CO of Pro and Nη2 of Arg is formed to fix the peptide. On the other hand, in the cis‐isomer, the formation of two hydrogen bonds of NH and CO of Ala preceding Pro with the protein fixes the peptide, whereas in the trans‐isomer formation of a hydrogen bond between CO preceding Ala‐Pro and His47 Nε2 via a mediating water molecule allows the large distortion in the orientation of Ala of Ala‐Pro. Although loss of double bond character of the amide bond of Ala‐Pro is essential to the isomerization pathway occurring by rotating around its bond, these peptides have forms impossible to undergo proton transfer from the guanidyl group of Arg to the prolyl N atom, which induces loss of double bond character.
doi_str_mv 10.1111/j.1432-1033.2004.04321.x
format Article
fullrecord <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_66862408</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>66862408</sourcerecordid><originalsourceid>FETCH-LOGICAL-c3971-31771a8b3788887a3fde424b914f1c0dc2ac9b3aff524f15c9c2a424072dbe373</originalsourceid><addsrcrecordid>eNqNkdFOwyAUhonRuDl9BcOVd61Q2tLemLhlU5MlXqiXhlBKLQsdFbq43vkIPqNPInWLXuoJCYfDdw7k_wGAGIXYx-UqxDGJAowICSOE4hD5Iw63B2D8c3EIxgjhOIjyJB2BE-dWCKE0T-kxGOGEJH6lY_A8d6KWVolacSiMVlD0Qpu2Vlqt4RQWal06yGGtXmrdw1K5zthOlrAytoGmgp3la_f5_tFao3sNW9l2qpRQOdNIewqOKq6dPNvvE_C0mD_OboPl_c3d7HoZCJJTHBBMKeZZQWjmg3JSlTKO4iLHcYUFKkXERV4QXlVJ5CuJyH3FA4hGZSEJJRNwsZvrf_G6ka5jjXJCas3X0mwcS9Ms9Xj2J4hpFqE8Ix7MdqCwxjkrK9Za1XDbM4zY4AFbsUFqNkjNBg_Ytwds61vP929sikaWv4170T1wtQPelJb9vwezxXz6MKTkCx7_lnI</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>17820983</pqid></control><display><type>article</type><title>Escherichia coli cyclophilin B binds a highly distorted form of trans‐prolyl peptide isomer</title><source>MEDLINE</source><source>Wiley Online Library</source><source>Alma/SFX Local Collection</source><creator>Konno, Michiko ; Sano, Yumi ; Okudaira, Kayoko ; Kawaguchi, Yoko ; Yamagishi‐Ohmori, Yoko ; Fushinobu, Shinya ; Matsuzawa, Hiroshi</creator><creatorcontrib>Konno, Michiko ; Sano, Yumi ; Okudaira, Kayoko ; Kawaguchi, Yoko ; Yamagishi‐Ohmori, Yoko ; Fushinobu, Shinya ; Matsuzawa, Hiroshi</creatorcontrib><description>Cyclophilins facilitate the peptidyl‐prolyl isomerization of a trans‐isomer to a cis‐isomer in the refolding process of unfolded proteins to recover the natural folding state with cis‐proline conformation. To date, only short peptides with a cis‐form proline have been observed in complexes of human and Escherichia coli proteins of cyclophilin A, which is present in cytoplasm. The crystal structures analyzed in this study show two complexes in which peptides having a trans‐form proline, i.e. succinyl‐Ala‐trans‐Pro‐Ala‐p‐nitroanilide and acetyl‐Ala‐Ala‐trans‐Pro‐Ala‐amidomethylcoumarin, are bound on a K163T mutant of Escherichia coli cyclophilin B, the preprotein of which has a signal sequence. Comparison with cis‐form peptides bound to cyclophilin A reveals that in any case the proline ring is inserted into the hydrophobic pocket and a hydrogen bond between CO of Pro and Nη2 of Arg is formed to fix the peptide. On the other hand, in the cis‐isomer, the formation of two hydrogen bonds of NH and CO of Ala preceding Pro with the protein fixes the peptide, whereas in the trans‐isomer formation of a hydrogen bond between CO preceding Ala‐Pro and His47 Nε2 via a mediating water molecule allows the large distortion in the orientation of Ala of Ala‐Pro. Although loss of double bond character of the amide bond of Ala‐Pro is essential to the isomerization pathway occurring by rotating around its bond, these peptides have forms impossible to undergo proton transfer from the guanidyl group of Arg to the prolyl N atom, which induces loss of double bond character.</description><identifier>ISSN: 0014-2956</identifier><identifier>EISSN: 1432-1033</identifier><identifier>DOI: 10.1111/j.1432-1033.2004.04321.x</identifier><identifier>PMID: 15355356</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Science Ltd</publisher><subject>Amino Acid Sequence ; Amino Acid Substitution ; Crystallization ; cyclophilin ; Cyclophilins - genetics ; Cyclophilins - metabolism ; Escherichia coli ; Escherichia coli - metabolism ; Hydrogen Bonding ; Isomerism ; isozyme ; Models, Molecular ; Molecular Sequence Data ; peptide binding ; Peptides - chemistry ; Peptides - genetics ; Peptidylprolyl Isomerase ; peptidyl‐prolyl cis‐trans isomerase ; Proline - chemistry ; Proline - genetics ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; refolding ; Sequence Homology, Amino Acid ; Threonine - metabolism</subject><ispartof>European journal of biochemistry, 2004-09, Vol.271 (18), p.3794-3803</ispartof><rights>Copyright 2004 FEBS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3971-31771a8b3788887a3fde424b914f1c0dc2ac9b3aff524f15c9c2a424072dbe373</citedby><cites>FETCH-LOGICAL-c3971-31771a8b3788887a3fde424b914f1c0dc2ac9b3aff524f15c9c2a424072dbe373</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1111%2Fj.1432-1033.2004.04321.x$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1111%2Fj.1432-1033.2004.04321.x$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,776,780,1411,27901,27902,45550,45551</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15355356$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Konno, Michiko</creatorcontrib><creatorcontrib>Sano, Yumi</creatorcontrib><creatorcontrib>Okudaira, Kayoko</creatorcontrib><creatorcontrib>Kawaguchi, Yoko</creatorcontrib><creatorcontrib>Yamagishi‐Ohmori, Yoko</creatorcontrib><creatorcontrib>Fushinobu, Shinya</creatorcontrib><creatorcontrib>Matsuzawa, Hiroshi</creatorcontrib><title>Escherichia coli cyclophilin B binds a highly distorted form of trans‐prolyl peptide isomer</title><title>European journal of biochemistry</title><addtitle>Eur J Biochem</addtitle><description>Cyclophilins facilitate the peptidyl‐prolyl isomerization of a trans‐isomer to a cis‐isomer in the refolding process of unfolded proteins to recover the natural folding state with cis‐proline conformation. To date, only short peptides with a cis‐form proline have been observed in complexes of human and Escherichia coli proteins of cyclophilin A, which is present in cytoplasm. The crystal structures analyzed in this study show two complexes in which peptides having a trans‐form proline, i.e. succinyl‐Ala‐trans‐Pro‐Ala‐p‐nitroanilide and acetyl‐Ala‐Ala‐trans‐Pro‐Ala‐amidomethylcoumarin, are bound on a K163T mutant of Escherichia coli cyclophilin B, the preprotein of which has a signal sequence. Comparison with cis‐form peptides bound to cyclophilin A reveals that in any case the proline ring is inserted into the hydrophobic pocket and a hydrogen bond between CO of Pro and Nη2 of Arg is formed to fix the peptide. On the other hand, in the cis‐isomer, the formation of two hydrogen bonds of NH and CO of Ala preceding Pro with the protein fixes the peptide, whereas in the trans‐isomer formation of a hydrogen bond between CO preceding Ala‐Pro and His47 Nε2 via a mediating water molecule allows the large distortion in the orientation of Ala of Ala‐Pro. Although loss of double bond character of the amide bond of Ala‐Pro is essential to the isomerization pathway occurring by rotating around its bond, these peptides have forms impossible to undergo proton transfer from the guanidyl group of Arg to the prolyl N atom, which induces loss of double bond character.</description><subject>Amino Acid Sequence</subject><subject>Amino Acid Substitution</subject><subject>Crystallization</subject><subject>cyclophilin</subject><subject>Cyclophilins - genetics</subject><subject>Cyclophilins - metabolism</subject><subject>Escherichia coli</subject><subject>Escherichia coli - metabolism</subject><subject>Hydrogen Bonding</subject><subject>Isomerism</subject><subject>isozyme</subject><subject>Models, Molecular</subject><subject>Molecular Sequence Data</subject><subject>peptide binding</subject><subject>Peptides - chemistry</subject><subject>Peptides - genetics</subject><subject>Peptidylprolyl Isomerase</subject><subject>peptidyl‐prolyl cis‐trans isomerase</subject><subject>Proline - chemistry</subject><subject>Proline - genetics</subject><subject>Protein Conformation</subject><subject>Protein Folding</subject><subject>Protein Structure, Secondary</subject><subject>refolding</subject><subject>Sequence Homology, Amino Acid</subject><subject>Threonine - metabolism</subject><issn>0014-2956</issn><issn>1432-1033</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkdFOwyAUhonRuDl9BcOVd61Q2tLemLhlU5MlXqiXhlBKLQsdFbq43vkIPqNPInWLXuoJCYfDdw7k_wGAGIXYx-UqxDGJAowICSOE4hD5Iw63B2D8c3EIxgjhOIjyJB2BE-dWCKE0T-kxGOGEJH6lY_A8d6KWVolacSiMVlD0Qpu2Vlqt4RQWal06yGGtXmrdw1K5zthOlrAytoGmgp3la_f5_tFao3sNW9l2qpRQOdNIewqOKq6dPNvvE_C0mD_OboPl_c3d7HoZCJJTHBBMKeZZQWjmg3JSlTKO4iLHcYUFKkXERV4QXlVJ5CuJyH3FA4hGZSEJJRNwsZvrf_G6ka5jjXJCas3X0mwcS9Ms9Xj2J4hpFqE8Ix7MdqCwxjkrK9Za1XDbM4zY4AFbsUFqNkjNBg_Ytwds61vP929sikaWv4170T1wtQPelJb9vwezxXz6MKTkCx7_lnI</recordid><startdate>200409</startdate><enddate>200409</enddate><creator>Konno, Michiko</creator><creator>Sano, Yumi</creator><creator>Okudaira, Kayoko</creator><creator>Kawaguchi, Yoko</creator><creator>Yamagishi‐Ohmori, Yoko</creator><creator>Fushinobu, Shinya</creator><creator>Matsuzawa, Hiroshi</creator><general>Blackwell Science Ltd</general><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></search><sort><creationdate>200409</creationdate><title>Escherichia coli cyclophilin B binds a highly distorted form of trans‐prolyl peptide isomer</title><author>Konno, Michiko ; Sano, Yumi ; Okudaira, Kayoko ; Kawaguchi, Yoko ; Yamagishi‐Ohmori, Yoko ; Fushinobu, Shinya ; Matsuzawa, Hiroshi</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3971-31771a8b3788887a3fde424b914f1c0dc2ac9b3aff524f15c9c2a424072dbe373</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2004</creationdate><topic>Amino Acid Sequence</topic><topic>Amino Acid Substitution</topic><topic>Crystallization</topic><topic>cyclophilin</topic><topic>Cyclophilins - genetics</topic><topic>Cyclophilins - metabolism</topic><topic>Escherichia coli</topic><topic>Escherichia coli - metabolism</topic><topic>Hydrogen Bonding</topic><topic>Isomerism</topic><topic>isozyme</topic><topic>Models, Molecular</topic><topic>Molecular Sequence Data</topic><topic>peptide binding</topic><topic>Peptides - chemistry</topic><topic>Peptides - genetics</topic><topic>Peptidylprolyl Isomerase</topic><topic>peptidyl‐prolyl cis‐trans isomerase</topic><topic>Proline - chemistry</topic><topic>Proline - genetics</topic><topic>Protein Conformation</topic><topic>Protein Folding</topic><topic>Protein Structure, Secondary</topic><topic>refolding</topic><topic>Sequence Homology, Amino Acid</topic><topic>Threonine - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Konno, Michiko</creatorcontrib><creatorcontrib>Sano, Yumi</creatorcontrib><creatorcontrib>Okudaira, Kayoko</creatorcontrib><creatorcontrib>Kawaguchi, Yoko</creatorcontrib><creatorcontrib>Yamagishi‐Ohmori, Yoko</creatorcontrib><creatorcontrib>Fushinobu, Shinya</creatorcontrib><creatorcontrib>Matsuzawa, Hiroshi</creatorcontrib><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><jtitle>European journal of biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Konno, Michiko</au><au>Sano, Yumi</au><au>Okudaira, Kayoko</au><au>Kawaguchi, Yoko</au><au>Yamagishi‐Ohmori, Yoko</au><au>Fushinobu, Shinya</au><au>Matsuzawa, Hiroshi</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Escherichia coli cyclophilin B binds a highly distorted form of trans‐prolyl peptide isomer</atitle><jtitle>European journal of biochemistry</jtitle><addtitle>Eur J Biochem</addtitle><date>2004-09</date><risdate>2004</risdate><volume>271</volume><issue>18</issue><spage>3794</spage><epage>3803</epage><pages>3794-3803</pages><issn>0014-2956</issn><eissn>1432-1033</eissn><abstract>Cyclophilins facilitate the peptidyl‐prolyl isomerization of a trans‐isomer to a cis‐isomer in the refolding process of unfolded proteins to recover the natural folding state with cis‐proline conformation. To date, only short peptides with a cis‐form proline have been observed in complexes of human and Escherichia coli proteins of cyclophilin A, which is present in cytoplasm. The crystal structures analyzed in this study show two complexes in which peptides having a trans‐form proline, i.e. succinyl‐Ala‐trans‐Pro‐Ala‐p‐nitroanilide and acetyl‐Ala‐Ala‐trans‐Pro‐Ala‐amidomethylcoumarin, are bound on a K163T mutant of Escherichia coli cyclophilin B, the preprotein of which has a signal sequence. Comparison with cis‐form peptides bound to cyclophilin A reveals that in any case the proline ring is inserted into the hydrophobic pocket and a hydrogen bond between CO of Pro and Nη2 of Arg is formed to fix the peptide. On the other hand, in the cis‐isomer, the formation of two hydrogen bonds of NH and CO of Ala preceding Pro with the protein fixes the peptide, whereas in the trans‐isomer formation of a hydrogen bond between CO preceding Ala‐Pro and His47 Nε2 via a mediating water molecule allows the large distortion in the orientation of Ala of Ala‐Pro. Although loss of double bond character of the amide bond of Ala‐Pro is essential to the isomerization pathway occurring by rotating around its bond, these peptides have forms impossible to undergo proton transfer from the guanidyl group of Arg to the prolyl N atom, which induces loss of double bond character.</abstract><cop>Oxford, UK</cop><pub>Blackwell Science Ltd</pub><pmid>15355356</pmid><doi>10.1111/j.1432-1033.2004.04321.x</doi><tpages>10</tpages></addata></record>
fulltext fulltext
identifier ISSN: 0014-2956
ispartof European journal of biochemistry, 2004-09, Vol.271 (18), p.3794-3803
issn 0014-2956
1432-1033
language eng
recordid cdi_proquest_miscellaneous_66862408
source MEDLINE; Wiley Online Library; Alma/SFX Local Collection
subjects Amino Acid Sequence
Amino Acid Substitution
Crystallization
cyclophilin
Cyclophilins - genetics
Cyclophilins - metabolism
Escherichia coli
Escherichia coli - metabolism
Hydrogen Bonding
Isomerism
isozyme
Models, Molecular
Molecular Sequence Data
peptide binding
Peptides - chemistry
Peptides - genetics
Peptidylprolyl Isomerase
peptidyl‐prolyl cis‐trans isomerase
Proline - chemistry
Proline - genetics
Protein Conformation
Protein Folding
Protein Structure, Secondary
refolding
Sequence Homology, Amino Acid
Threonine - metabolism
title Escherichia coli cyclophilin B binds a highly distorted form of trans‐prolyl peptide isomer
url https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-14T19%3A12%3A51IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Escherichia%20coli%20cyclophilin%20B%20binds%20a%20highly%20distorted%20form%20of%20trans%E2%80%90prolyl%20peptide%20isomer&rft.jtitle=European%20journal%20of%20biochemistry&rft.au=Konno,%20Michiko&rft.date=2004-09&rft.volume=271&rft.issue=18&rft.spage=3794&rft.epage=3803&rft.pages=3794-3803&rft.issn=0014-2956&rft.eissn=1432-1033&rft_id=info:doi/10.1111/j.1432-1033.2004.04321.x&rft_dat=%3Cproquest_cross%3E66862408%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=17820983&rft_id=info:pmid/15355356&rfr_iscdi=true