Acyl carrier protein structural classification and normal mode analysis

All acyl carrier protein primary and tertiary structures were gathered into the ThYme database. They are classified into 16 families by amino acid sequence similarity, with members of the different families having sequences with statistically highly significant differences. These classifications are...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:Protein science 2012-05, Vol.21 (5), p.655-666
Hauptverfasser: Cantu, David C., Forrester, Michael J., Charov, Katherine, Reilly, Peter J.
Format: Artikel
Sprache:eng
Schlagworte:
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
container_end_page 666
container_issue 5
container_start_page 655
container_title Protein science
container_volume 21
creator Cantu, David C.
Forrester, Michael J.
Charov, Katherine
Reilly, Peter J.
description All acyl carrier protein primary and tertiary structures were gathered into the ThYme database. They are classified into 16 families by amino acid sequence similarity, with members of the different families having sequences with statistically highly significant differences. These classifications are supported by tertiary structure superposition analysis. Tertiary structures from a number of families are very similar, suggesting that these families may come from a single distant ancestor. Normal vibrational mode analysis was conducted on experimentally determined freestanding structures, showing greater fluctuations at chain termini and loops than in most helices. Their modes overlap more so within families than between different families. The tertiary structures of three acyl carrier protein families that lacked any known structures were predicted as well.
doi_str_mv 10.1002/pro.2050
format Article
fullrecord <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_3403463</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>3958280991</sourcerecordid><originalsourceid>FETCH-LOGICAL-c4370-e9f142b3e2a1c94a7d4211891f5916b3d553cf32fbe4ed5c944a4aed2b8d17213</originalsourceid><addsrcrecordid>eNp1kV1LwzAYhYMobk7BXyAFL_SmM19tkxthDJ3CQBEF70KapprRNjNplf57MzeHCl6Fl_PwcMIB4BjBMYIQXyydHWOYwB0wRDTlMePp8y4YQp6imJGUDcCB9wsIIUWY7IMBxiSjLOFDMJuovoqUdM5oFwVPq00T-dZ1qu2cDFElvTelUbI1tolkU0SNdXVIalvocMuq98Yfgr1SVl4fbd4ReLq-epzexPO72e10Mo8VJRmMNS8RxTnRWCLFqcwKihFiHJUJR2lOiiQhqiS4zDXVRRIQKqnUBc5ZgTKMyAhcrr3LLq91oXTThpZi6UwtXS-sNOJ30phX8WLfBaGQ0JQEwdlG4Oxbp30rauOVrirZaNt5wTnhkDNCA3n6h1zYzoX_eoGyNGUUMcwCdb6mlLPeO11uuyAoVuOE24rVOAE9-dl9C36vEYB4DXyYSvf_isT9w92X8BPkPZnJ</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1766841828</pqid></control><display><type>article</type><title>Acyl carrier protein structural classification and normal mode analysis</title><source>MEDLINE</source><source>Access via Wiley Online Library</source><source>EZB-FREE-00999 freely available EZB journals</source><source>Wiley Online Library (Open Access Collection)</source><source>PubMed Central</source><source>Free Full-Text Journals in Chemistry</source><creator>Cantu, David C. ; Forrester, Michael J. ; Charov, Katherine ; Reilly, Peter J.</creator><creatorcontrib>Cantu, David C. ; Forrester, Michael J. ; Charov, Katherine ; Reilly, Peter J.</creatorcontrib><description>All acyl carrier protein primary and tertiary structures were gathered into the ThYme database. They are classified into 16 families by amino acid sequence similarity, with members of the different families having sequences with statistically highly significant differences. These classifications are supported by tertiary structure superposition analysis. Tertiary structures from a number of families are very similar, suggesting that these families may come from a single distant ancestor. Normal vibrational mode analysis was conducted on experimentally determined freestanding structures, showing greater fluctuations at chain termini and loops than in most helices. Their modes overlap more so within families than between different families. The tertiary structures of three acyl carrier protein families that lacked any known structures were predicted as well.</description><identifier>ISSN: 0961-8368</identifier><identifier>EISSN: 1469-896X</identifier><identifier>DOI: 10.1002/pro.2050</identifier><identifier>PMID: 22374859</identifier><identifier>CODEN: PRCIEI</identifier><language>eng</language><publisher>Hoboken: Wiley Subscription Services, Inc., A Wiley Company</publisher><subject>acyl carrier protein ; Acyl Carrier Protein - chemistry ; Acyl Carrier Protein - classification ; Amino Acid Sequence ; Animals ; Avian Proteins - chemistry ; Bacterial Proteins - chemistry ; Chickens ; Fungal Proteins - chemistry ; Humans ; Meat processing ; Models, Molecular ; Molecular Sequence Data ; normal mode analysis ; Phylogeny ; primary structure ; protein family ; Protein Structure, Tertiary ; Proteins ; Sequence Alignment ; tertiary structure ; ThYme</subject><ispartof>Protein science, 2012-05, Vol.21 (5), p.655-666</ispartof><rights>Copyright © 2012 The Protein Society</rights><rights>Copyright © 2012 The Protein Society.</rights><rights>Copyright © 2012 The Protein Society 2012</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4370-e9f142b3e2a1c94a7d4211891f5916b3d553cf32fbe4ed5c944a4aed2b8d17213</citedby><cites>FETCH-LOGICAL-c4370-e9f142b3e2a1c94a7d4211891f5916b3d553cf32fbe4ed5c944a4aed2b8d17213</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3403463/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3403463/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,727,780,784,885,1417,1433,27924,27925,45574,45575,46409,46833,53791,53793</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/22374859$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Cantu, David C.</creatorcontrib><creatorcontrib>Forrester, Michael J.</creatorcontrib><creatorcontrib>Charov, Katherine</creatorcontrib><creatorcontrib>Reilly, Peter J.</creatorcontrib><title>Acyl carrier protein structural classification and normal mode analysis</title><title>Protein science</title><addtitle>Protein Sci</addtitle><description>All acyl carrier protein primary and tertiary structures were gathered into the ThYme database. They are classified into 16 families by amino acid sequence similarity, with members of the different families having sequences with statistically highly significant differences. These classifications are supported by tertiary structure superposition analysis. Tertiary structures from a number of families are very similar, suggesting that these families may come from a single distant ancestor. Normal vibrational mode analysis was conducted on experimentally determined freestanding structures, showing greater fluctuations at chain termini and loops than in most helices. Their modes overlap more so within families than between different families. The tertiary structures of three acyl carrier protein families that lacked any known structures were predicted as well.</description><subject>acyl carrier protein</subject><subject>Acyl Carrier Protein - chemistry</subject><subject>Acyl Carrier Protein - classification</subject><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Avian Proteins - chemistry</subject><subject>Bacterial Proteins - chemistry</subject><subject>Chickens</subject><subject>Fungal Proteins - chemistry</subject><subject>Humans</subject><subject>Meat processing</subject><subject>Models, Molecular</subject><subject>Molecular Sequence Data</subject><subject>normal mode analysis</subject><subject>Phylogeny</subject><subject>primary structure</subject><subject>protein family</subject><subject>Protein Structure, Tertiary</subject><subject>Proteins</subject><subject>Sequence Alignment</subject><subject>tertiary structure</subject><subject>ThYme</subject><issn>0961-8368</issn><issn>1469-896X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2012</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kV1LwzAYhYMobk7BXyAFL_SmM19tkxthDJ3CQBEF70KapprRNjNplf57MzeHCl6Fl_PwcMIB4BjBMYIQXyydHWOYwB0wRDTlMePp8y4YQp6imJGUDcCB9wsIIUWY7IMBxiSjLOFDMJuovoqUdM5oFwVPq00T-dZ1qu2cDFElvTelUbI1tolkU0SNdXVIalvocMuq98Yfgr1SVl4fbd4ReLq-epzexPO72e10Mo8VJRmMNS8RxTnRWCLFqcwKihFiHJUJR2lOiiQhqiS4zDXVRRIQKqnUBc5ZgTKMyAhcrr3LLq91oXTThpZi6UwtXS-sNOJ30phX8WLfBaGQ0JQEwdlG4Oxbp30rauOVrirZaNt5wTnhkDNCA3n6h1zYzoX_eoGyNGUUMcwCdb6mlLPeO11uuyAoVuOE24rVOAE9-dl9C36vEYB4DXyYSvf_isT9w92X8BPkPZnJ</recordid><startdate>201205</startdate><enddate>201205</enddate><creator>Cantu, David C.</creator><creator>Forrester, Michael J.</creator><creator>Charov, Katherine</creator><creator>Reilly, Peter J.</creator><general>Wiley Subscription Services, Inc., A Wiley Company</general><general>Wiley Subscription Services, Inc</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>7QO</scope><scope>7T5</scope><scope>7TM</scope><scope>7U9</scope><scope>8FD</scope><scope>FR3</scope><scope>H94</scope><scope>K9.</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>201205</creationdate><title>Acyl carrier protein structural classification and normal mode analysis</title><author>Cantu, David C. ; Forrester, Michael J. ; Charov, Katherine ; Reilly, Peter J.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4370-e9f142b3e2a1c94a7d4211891f5916b3d553cf32fbe4ed5c944a4aed2b8d17213</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2012</creationdate><topic>acyl carrier protein</topic><topic>Acyl Carrier Protein - chemistry</topic><topic>Acyl Carrier Protein - classification</topic><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Avian Proteins - chemistry</topic><topic>Bacterial Proteins - chemistry</topic><topic>Chickens</topic><topic>Fungal Proteins - chemistry</topic><topic>Humans</topic><topic>Meat processing</topic><topic>Models, Molecular</topic><topic>Molecular Sequence Data</topic><topic>normal mode analysis</topic><topic>Phylogeny</topic><topic>primary structure</topic><topic>protein family</topic><topic>Protein Structure, Tertiary</topic><topic>Proteins</topic><topic>Sequence Alignment</topic><topic>tertiary structure</topic><topic>ThYme</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Cantu, David C.</creatorcontrib><creatorcontrib>Forrester, Michael J.</creatorcontrib><creatorcontrib>Charov, Katherine</creatorcontrib><creatorcontrib>Reilly, Peter J.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Biotechnology Research Abstracts</collection><collection>Immunology Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>ProQuest Health &amp; Medical Complete (Alumni)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Protein science</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Cantu, David C.</au><au>Forrester, Michael J.</au><au>Charov, Katherine</au><au>Reilly, Peter J.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Acyl carrier protein structural classification and normal mode analysis</atitle><jtitle>Protein science</jtitle><addtitle>Protein Sci</addtitle><date>2012-05</date><risdate>2012</risdate><volume>21</volume><issue>5</issue><spage>655</spage><epage>666</epage><pages>655-666</pages><issn>0961-8368</issn><eissn>1469-896X</eissn><coden>PRCIEI</coden><abstract>All acyl carrier protein primary and tertiary structures were gathered into the ThYme database. They are classified into 16 families by amino acid sequence similarity, with members of the different families having sequences with statistically highly significant differences. These classifications are supported by tertiary structure superposition analysis. Tertiary structures from a number of families are very similar, suggesting that these families may come from a single distant ancestor. Normal vibrational mode analysis was conducted on experimentally determined freestanding structures, showing greater fluctuations at chain termini and loops than in most helices. Their modes overlap more so within families than between different families. The tertiary structures of three acyl carrier protein families that lacked any known structures were predicted as well.</abstract><cop>Hoboken</cop><pub>Wiley Subscription Services, Inc., A Wiley Company</pub><pmid>22374859</pmid><doi>10.1002/pro.2050</doi><tpages>12</tpages><oa>free_for_read</oa></addata></record>
fulltext fulltext
identifier ISSN: 0961-8368
ispartof Protein science, 2012-05, Vol.21 (5), p.655-666
issn 0961-8368
1469-896X
language eng
recordid cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_3403463
source MEDLINE; Access via Wiley Online Library; EZB-FREE-00999 freely available EZB journals; Wiley Online Library (Open Access Collection); PubMed Central; Free Full-Text Journals in Chemistry
subjects acyl carrier protein
Acyl Carrier Protein - chemistry
Acyl Carrier Protein - classification
Amino Acid Sequence
Animals
Avian Proteins - chemistry
Bacterial Proteins - chemistry
Chickens
Fungal Proteins - chemistry
Humans
Meat processing
Models, Molecular
Molecular Sequence Data
normal mode analysis
Phylogeny
primary structure
protein family
Protein Structure, Tertiary
Proteins
Sequence Alignment
tertiary structure
ThYme
title Acyl carrier protein structural classification and normal mode analysis
url https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-29T03%3A24%3A15IST&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=Acyl%20carrier%20protein%20structural%20classification%20and%20normal%20mode%20analysis&rft.jtitle=Protein%20science&rft.au=Cantu,%20David%20C.&rft.date=2012-05&rft.volume=21&rft.issue=5&rft.spage=655&rft.epage=666&rft.pages=655-666&rft.issn=0961-8368&rft.eissn=1469-896X&rft.coden=PRCIEI&rft_id=info:doi/10.1002/pro.2050&rft_dat=%3Cproquest_pubme%3E3958280991%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=1766841828&rft_id=info:pmid/22374859&rfr_iscdi=true