Crystal structures of Escherichia coli phytase and its complex with phytate
Phytases catalyze the hydrolysis of phytate and are able to improve the nutritional quality of phytate-rich diets. Escherichia coli phytase, a member of the histidine acid phosphatase family has the highest specific activity of all phytases characterized. The crystal structure of E. coli phytase has...
Gespeichert in:
| Veröffentlicht in: | Nature Structural Biology 2000-02, Vol.7 (2), p.108-113 |
|---|---|
| Hauptverfasser: | , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 113 |
|---|---|
| container_issue | 2 |
| container_start_page | 108 |
| container_title | Nature Structural Biology |
| container_volume | 7 |
| creator | Jia, Zongchao Lim, Daniel Golovan, Serguei Forsberg, Cecil W |
| description | Phytases catalyze the hydrolysis of phytate and are able to improve the nutritional quality of phytate-rich diets.
Escherichia coli
phytase, a member of the histidine acid phosphatase family has the highest specific activity of all phytases characterized. The crystal structure of
E. coli
phytase has been determined by a two-wavelength anomalous diffraction method using the exceptionally strong anomalous scattering of tungsten. Despite a lack of sequence similarity, the structure closely resembles the overall fold of other histidine acid phosphatases. The structure of
E. coli
phytase in complex with phytate, the preferred substrate, reveals the binding mode and substrate recognition. The binding is also accompanied by conformational changes which suggest that substrate binding enhances catalysis by increasing the acidity of the general acid. |
| doi_str_mv | 10.1038/72371 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_proquest_miscellaneous_70875265</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>70875265</sourcerecordid><originalsourceid>FETCH-LOGICAL-c358t-1e7b45f10a56e4364135bfa0021fa05a4462f3abaf1a372c60d9451ab047f99f3</originalsourceid><addsrcrecordid>eNqF0UtLw0AQB_BFFFtrv4JED96iM_tMjlLqAwteFLyFTboxKXm5u0H77U1tteDFyy7s_PgvM0PIFOEKgUXXijKFB2RMGcOQSfF6SMYIioYRk9GInDi3AkDOIT4mIwQphEQck8eZXTuvq8B522e-t8YFbR7MXVYYW2ZFqYOsrcqgK9ZeOxPoZhmU3g2PdVeZz-Cj9MW26M0pOcp15cx0d0_Iy-38eXYfLp7uHmY3izBjIvIhGpVykSNoIQ1nkiMTaa4BKA6n0JxLmjOd6hw1UzSTsIy5QJ0CV3kc52xCLre5nW3fe-N8UpcuM1WlG9P2LlEQKUGl-BeiGihwOcCLP3DV9rYZmkgojWgUMxYP6GyH-rQ2y6SzZa3tOvkZ5v47N5SaN2P3KQjJZkvJ95YGeL6Fjd5M_DepcSlQ2NCIfQFKt4rZ</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>228289339</pqid></control><display><type>article</type><title>Crystal structures of Escherichia coli phytase and its complex with phytate</title><source>MEDLINE</source><source>Nature</source><source>Alma/SFX Local Collection</source><creator>Jia, Zongchao ; Lim, Daniel ; Golovan, Serguei ; Forsberg, Cecil W</creator><creatorcontrib>Jia, Zongchao ; Lim, Daniel ; Golovan, Serguei ; Forsberg, Cecil W</creatorcontrib><description>Phytases catalyze the hydrolysis of phytate and are able to improve the nutritional quality of phytate-rich diets.
Escherichia coli
phytase, a member of the histidine acid phosphatase family has the highest specific activity of all phytases characterized. The crystal structure of
E. coli
phytase has been determined by a two-wavelength anomalous diffraction method using the exceptionally strong anomalous scattering of tungsten. Despite a lack of sequence similarity, the structure closely resembles the overall fold of other histidine acid phosphatases. The structure of
E. coli
phytase in complex with phytate, the preferred substrate, reveals the binding mode and substrate recognition. The binding is also accompanied by conformational changes which suggest that substrate binding enhances catalysis by increasing the acidity of the general acid.</description><identifier>ISSN: 1072-8368</identifier><identifier>ISSN: 1545-9993</identifier><identifier>EISSN: 2331-365X</identifier><identifier>EISSN: 1545-9985</identifier><identifier>DOI: 10.1038/72371</identifier><identifier>PMID: 10655611</identifier><language>eng</language><publisher>New York: Nature Publishing Group US</publisher><subject>6-Phytase - chemistry ; 6-Phytase - genetics ; 6-Phytase - metabolism ; Acidity ; Amino Acid Motifs ; Bacterial Proteins - chemistry ; Bacterial Proteins - metabolism ; Binding Sites ; Biochemistry ; Biological Microscopy ; Biomedical and Life Sciences ; Catalysis ; Crystallography, X-Ray ; E coli ; Escherichia coli ; Escherichia coli - enzymology ; letter ; Life Sciences ; Membrane Biology ; Models, Molecular ; Mutation ; Nutritive value ; phytic acid ; Phytic Acid - chemistry ; Phytic Acid - metabolism ; Protein Conformation ; Protein Structure ; Tungsten</subject><ispartof>Nature Structural Biology, 2000-02, Vol.7 (2), p.108-113</ispartof><rights>Nature America Inc. 2000</rights><rights>Copyright Nature Publishing Group Feb 2000</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c358t-1e7b45f10a56e4364135bfa0021fa05a4462f3abaf1a372c60d9451ab047f99f3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,2727,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10655611$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Jia, Zongchao</creatorcontrib><creatorcontrib>Lim, Daniel</creatorcontrib><creatorcontrib>Golovan, Serguei</creatorcontrib><creatorcontrib>Forsberg, Cecil W</creatorcontrib><title>Crystal structures of Escherichia coli phytase and its complex with phytate</title><title>Nature Structural Biology</title><addtitle>Nat Struct Mol Biol</addtitle><addtitle>Nat Struct Biol</addtitle><description>Phytases catalyze the hydrolysis of phytate and are able to improve the nutritional quality of phytate-rich diets.
Escherichia coli
phytase, a member of the histidine acid phosphatase family has the highest specific activity of all phytases characterized. The crystal structure of
E. coli
phytase has been determined by a two-wavelength anomalous diffraction method using the exceptionally strong anomalous scattering of tungsten. Despite a lack of sequence similarity, the structure closely resembles the overall fold of other histidine acid phosphatases. The structure of
E. coli
phytase in complex with phytate, the preferred substrate, reveals the binding mode and substrate recognition. The binding is also accompanied by conformational changes which suggest that substrate binding enhances catalysis by increasing the acidity of the general acid.</description><subject>6-Phytase - chemistry</subject><subject>6-Phytase - genetics</subject><subject>6-Phytase - metabolism</subject><subject>Acidity</subject><subject>Amino Acid Motifs</subject><subject>Bacterial Proteins - chemistry</subject><subject>Bacterial Proteins - metabolism</subject><subject>Binding Sites</subject><subject>Biochemistry</subject><subject>Biological Microscopy</subject><subject>Biomedical and Life Sciences</subject><subject>Catalysis</subject><subject>Crystallography, X-Ray</subject><subject>E coli</subject><subject>Escherichia coli</subject><subject>Escherichia coli - enzymology</subject><subject>letter</subject><subject>Life Sciences</subject><subject>Membrane Biology</subject><subject>Models, Molecular</subject><subject>Mutation</subject><subject>Nutritive value</subject><subject>phytic acid</subject><subject>Phytic Acid - chemistry</subject><subject>Phytic Acid - metabolism</subject><subject>Protein Conformation</subject><subject>Protein Structure</subject><subject>Tungsten</subject><issn>1072-8368</issn><issn>1545-9993</issn><issn>2331-365X</issn><issn>1545-9985</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2000</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNqF0UtLw0AQB_BFFFtrv4JED96iM_tMjlLqAwteFLyFTboxKXm5u0H77U1tteDFyy7s_PgvM0PIFOEKgUXXijKFB2RMGcOQSfF6SMYIioYRk9GInDi3AkDOIT4mIwQphEQck8eZXTuvq8B522e-t8YFbR7MXVYYW2ZFqYOsrcqgK9ZeOxPoZhmU3g2PdVeZz-Cj9MW26M0pOcp15cx0d0_Iy-38eXYfLp7uHmY3izBjIvIhGpVykSNoIQ1nkiMTaa4BKA6n0JxLmjOd6hw1UzSTsIy5QJ0CV3kc52xCLre5nW3fe-N8UpcuM1WlG9P2LlEQKUGl-BeiGihwOcCLP3DV9rYZmkgojWgUMxYP6GyH-rQ2y6SzZa3tOvkZ5v47N5SaN2P3KQjJZkvJ95YGeL6Fjd5M_DepcSlQ2NCIfQFKt4rZ</recordid><startdate>20000201</startdate><enddate>20000201</enddate><creator>Jia, Zongchao</creator><creator>Lim, Daniel</creator><creator>Golovan, Serguei</creator><creator>Forsberg, Cecil W</creator><general>Nature Publishing Group US</general><general>Nature Publishing Group</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>3V.</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>8AO</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>M7N</scope><scope>M7P</scope><scope>MBDVC</scope><scope>P64</scope><scope>PADUT</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>20000201</creationdate><title>Crystal structures of Escherichia coli phytase and its complex with phytate</title><author>Jia, Zongchao ; Lim, Daniel ; Golovan, Serguei ; Forsberg, Cecil W</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c358t-1e7b45f10a56e4364135bfa0021fa05a4462f3abaf1a372c60d9451ab047f99f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2000</creationdate><topic>6-Phytase - chemistry</topic><topic>6-Phytase - genetics</topic><topic>6-Phytase - metabolism</topic><topic>Acidity</topic><topic>Amino Acid Motifs</topic><topic>Bacterial Proteins - chemistry</topic><topic>Bacterial Proteins - metabolism</topic><topic>Binding Sites</topic><topic>Biochemistry</topic><topic>Biological Microscopy</topic><topic>Biomedical and Life Sciences</topic><topic>Catalysis</topic><topic>Crystallography, X-Ray</topic><topic>E coli</topic><topic>Escherichia coli</topic><topic>Escherichia coli - enzymology</topic><topic>letter</topic><topic>Life Sciences</topic><topic>Membrane Biology</topic><topic>Models, Molecular</topic><topic>Mutation</topic><topic>Nutritive value</topic><topic>phytic acid</topic><topic>Phytic Acid - chemistry</topic><topic>Phytic Acid - metabolism</topic><topic>Protein Conformation</topic><topic>Protein Structure</topic><topic>Tungsten</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Jia, Zongchao</creatorcontrib><creatorcontrib>Lim, Daniel</creatorcontrib><creatorcontrib>Golovan, Serguei</creatorcontrib><creatorcontrib>Forsberg, Cecil W</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>ProQuest Central (Corporate)</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Research Library (Alumni Edition)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>Research Library Prep</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Research Library</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Research Library (Corporate)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Research Library China</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central Basic</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Nature Structural Biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Jia, Zongchao</au><au>Lim, Daniel</au><au>Golovan, Serguei</au><au>Forsberg, Cecil W</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Crystal structures of Escherichia coli phytase and its complex with phytate</atitle><jtitle>Nature Structural Biology</jtitle><stitle>Nat Struct Mol Biol</stitle><addtitle>Nat Struct Biol</addtitle><date>2000-02-01</date><risdate>2000</risdate><volume>7</volume><issue>2</issue><spage>108</spage><epage>113</epage><pages>108-113</pages><issn>1072-8368</issn><issn>1545-9993</issn><eissn>2331-365X</eissn><eissn>1545-9985</eissn><abstract>Phytases catalyze the hydrolysis of phytate and are able to improve the nutritional quality of phytate-rich diets.
Escherichia coli
phytase, a member of the histidine acid phosphatase family has the highest specific activity of all phytases characterized. The crystal structure of
E. coli
phytase has been determined by a two-wavelength anomalous diffraction method using the exceptionally strong anomalous scattering of tungsten. Despite a lack of sequence similarity, the structure closely resembles the overall fold of other histidine acid phosphatases. The structure of
E. coli
phytase in complex with phytate, the preferred substrate, reveals the binding mode and substrate recognition. The binding is also accompanied by conformational changes which suggest that substrate binding enhances catalysis by increasing the acidity of the general acid.</abstract><cop>New York</cop><pub>Nature Publishing Group US</pub><pmid>10655611</pmid><doi>10.1038/72371</doi><tpages>6</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 1072-8368 |
| ispartof | Nature Structural Biology, 2000-02, Vol.7 (2), p.108-113 |
| issn | 1072-8368 1545-9993 2331-365X 1545-9985 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_70875265 |
| source | MEDLINE; Nature; Alma/SFX Local Collection |
| subjects | 6-Phytase - chemistry 6-Phytase - genetics 6-Phytase - metabolism Acidity Amino Acid Motifs Bacterial Proteins - chemistry Bacterial Proteins - metabolism Binding Sites Biochemistry Biological Microscopy Biomedical and Life Sciences Catalysis Crystallography, X-Ray E coli Escherichia coli Escherichia coli - enzymology letter Life Sciences Membrane Biology Models, Molecular Mutation Nutritive value phytic acid Phytic Acid - chemistry Phytic Acid - metabolism Protein Conformation Protein Structure Tungsten |
| title | Crystal structures of Escherichia coli phytase and its complex with phytate |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-29T07%3A53%3A26IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Crystal%20structures%20of%20Escherichia%20coli%20phytase%20and%20its%20complex%20with%20phytate&rft.jtitle=Nature%20Structural%20Biology&rft.au=Jia,%20Zongchao&rft.date=2000-02-01&rft.volume=7&rft.issue=2&rft.spage=108&rft.epage=113&rft.pages=108-113&rft.issn=1072-8368&rft.eissn=2331-365X&rft_id=info:doi/10.1038/72371&rft_dat=%3Cproquest_pubme%3E70875265%3C/proquest_pubme%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=228289339&rft_id=info:pmid/10655611&rfr_iscdi=true |