Loading…
Crystallization and rhenium MAD phasing of the acyl-homoserinelactone synthase EsaI
Acyl-homoserine-L-lactones (AHLs) are diffusible chemical signals that are required for virulence of many Gram-negative bacteria. AHLs are produced by AHL synthases from two substrates, S-adenosyl-L-methionine and acyl-acyl carrier protein. The AHL synthase EsaI, which is homologous to the AHL synth...
Saved in:
| Published in: | Acta crystallographica. Section D, Biological crystallography. Biological crystallography., 2009-04, Vol.57 (2001) |
|---|---|
| Main Authors: | , , , , , , , |
| Format: | Article |
| Language: | English |
| Subjects: | |
| Online Access: | Get full text |
| Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
| cited_by | |
|---|---|
| cites | |
| container_end_page | |
| container_issue | 2001 |
| container_start_page | |
| container_title | Acta crystallographica. Section D, Biological crystallography. |
| container_volume | 57 |
| creator | Watson, W.T. Murphy IV, Frank V. Gould, Ty A. Jambeck, Per Val, Dale L. Cronan, Jr., John E. Beck von Bodman, Susan Churchill, Mair E.A. |
| description | Acyl-homoserine-L-lactones (AHLs) are diffusible chemical signals that are required for virulence of many Gram-negative bacteria. AHLs are produced by AHL synthases from two substrates, S-adenosyl-L-methionine and acyl-acyl carrier protein. The AHL synthase EsaI, which is homologous to the AHL synthases from other pathogenic bacterial species, has been crystallized in the primitive tetragonal space group P4{sub 3}, with unit-cell parameters a = b = 66.40, c = 47.33 {angstrom}. The structure was solved by multiple-wavelength anomalous diffraction with a novel use of the rhenium anomalous signal. The rhenium-containing structure has been refined to a resolution of 2.5 {angstrom} and the perrhenate ion binding sites and liganding residues have been identified. |
| format | article |
| fullrecord | <record><control><sourceid>osti</sourceid><recordid>TN_cdi_osti_scitechconnect_1006374</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>1006374</sourcerecordid><originalsourceid>FETCH-osti_scitechconnect_10063743</originalsourceid><addsrcrecordid>eNqNyr0KwjAQAOAgCtafdzjcC6cNlo5SFR2cdC8hniaSXqQXh_r0OvgATt_yDVS2LKoqR9TlUGVYYZlrrauxmog8EHG1KspMneuul2RC8G-TfGQwfIXOEftXC6fNFp7OiOc7xBskR2BsH3IX2yjUeaZgbIpMID2nbyTYiTnO1OhmgtD851Qt9rtLfcijJN-I9Ymss5GZbGqWiOui1MVf6QPxTkGJ</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype></control><display><type>article</type><title>Crystallization and rhenium MAD phasing of the acyl-homoserinelactone synthase EsaI</title><source>Wiley-Blackwell Read & Publish Collection</source><source>Alma/SFX Local Collection</source><creator>Watson, W.T. ; Murphy IV, Frank V. ; Gould, Ty A. ; Jambeck, Per ; Val, Dale L. ; Cronan, Jr., John E. ; Beck von Bodman, Susan ; Churchill, Mair E.A.</creator><creatorcontrib>Watson, W.T. ; Murphy IV, Frank V. ; Gould, Ty A. ; Jambeck, Per ; Val, Dale L. ; Cronan, Jr., John E. ; Beck von Bodman, Susan ; Churchill, Mair E.A. ; Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)</creatorcontrib><description>Acyl-homoserine-L-lactones (AHLs) are diffusible chemical signals that are required for virulence of many Gram-negative bacteria. AHLs are produced by AHL synthases from two substrates, S-adenosyl-L-methionine and acyl-acyl carrier protein. The AHL synthase EsaI, which is homologous to the AHL synthases from other pathogenic bacterial species, has been crystallized in the primitive tetragonal space group P4{sub 3}, with unit-cell parameters a = b = 66.40, c = 47.33 {angstrom}. The structure was solved by multiple-wavelength anomalous diffraction with a novel use of the rhenium anomalous signal. The rhenium-containing structure has been refined to a resolution of 2.5 {angstrom} and the perrhenate ion binding sites and liganding residues have been identified.</description><identifier>ISSN: 0907-4449</identifier><identifier>EISSN: 1399-0047</identifier><language>eng</language><publisher>United States</publisher><subject>BACTERIA ; BASIC BIOLOGICAL SCIENCES ; BIOLOGICAL FUNCTIONS ; CRYSTAL STRUCTURE ; CRYSTALLIZATION ; GENERAL AND MISCELLANEOUS//MATHEMATICS, COMPUTING, AND INFORMATION SCIENCE ; LACTONES ; PERRHENATES ; RHENIUM ; SPACE GROUPS ; VIRULENCE ; X-RAY DIFFRACTION</subject><ispartof>Acta crystallographica. Section D, Biological crystallography., 2009-04, Vol.57 (2001)</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,314,776,780,881</link.rule.ids><backlink>$$Uhttps://www.osti.gov/biblio/1006374$$D View this record in Osti.gov$$Hfree_for_read</backlink></links><search><creatorcontrib>Watson, W.T.</creatorcontrib><creatorcontrib>Murphy IV, Frank V.</creatorcontrib><creatorcontrib>Gould, Ty A.</creatorcontrib><creatorcontrib>Jambeck, Per</creatorcontrib><creatorcontrib>Val, Dale L.</creatorcontrib><creatorcontrib>Cronan, Jr., John E.</creatorcontrib><creatorcontrib>Beck von Bodman, Susan</creatorcontrib><creatorcontrib>Churchill, Mair E.A.</creatorcontrib><creatorcontrib>Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)</creatorcontrib><title>Crystallization and rhenium MAD phasing of the acyl-homoserinelactone synthase EsaI</title><title>Acta crystallographica. Section D, Biological crystallography.</title><description>Acyl-homoserine-L-lactones (AHLs) are diffusible chemical signals that are required for virulence of many Gram-negative bacteria. AHLs are produced by AHL synthases from two substrates, S-adenosyl-L-methionine and acyl-acyl carrier protein. The AHL synthase EsaI, which is homologous to the AHL synthases from other pathogenic bacterial species, has been crystallized in the primitive tetragonal space group P4{sub 3}, with unit-cell parameters a = b = 66.40, c = 47.33 {angstrom}. The structure was solved by multiple-wavelength anomalous diffraction with a novel use of the rhenium anomalous signal. The rhenium-containing structure has been refined to a resolution of 2.5 {angstrom} and the perrhenate ion binding sites and liganding residues have been identified.</description><subject>BACTERIA</subject><subject>BASIC BIOLOGICAL SCIENCES</subject><subject>BIOLOGICAL FUNCTIONS</subject><subject>CRYSTAL STRUCTURE</subject><subject>CRYSTALLIZATION</subject><subject>GENERAL AND MISCELLANEOUS//MATHEMATICS, COMPUTING, AND INFORMATION SCIENCE</subject><subject>LACTONES</subject><subject>PERRHENATES</subject><subject>RHENIUM</subject><subject>SPACE GROUPS</subject><subject>VIRULENCE</subject><subject>X-RAY DIFFRACTION</subject><issn>0907-4449</issn><issn>1399-0047</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2009</creationdate><recordtype>article</recordtype><recordid>eNqNyr0KwjAQAOAgCtafdzjcC6cNlo5SFR2cdC8hniaSXqQXh_r0OvgATt_yDVS2LKoqR9TlUGVYYZlrrauxmog8EHG1KspMneuul2RC8G-TfGQwfIXOEftXC6fNFp7OiOc7xBskR2BsH3IX2yjUeaZgbIpMID2nbyTYiTnO1OhmgtD851Qt9rtLfcijJN-I9Ymss5GZbGqWiOui1MVf6QPxTkGJ</recordid><startdate>20090422</startdate><enddate>20090422</enddate><creator>Watson, W.T.</creator><creator>Murphy IV, Frank V.</creator><creator>Gould, Ty A.</creator><creator>Jambeck, Per</creator><creator>Val, Dale L.</creator><creator>Cronan, Jr., John E.</creator><creator>Beck von Bodman, Susan</creator><creator>Churchill, Mair E.A.</creator><scope>OTOTI</scope></search><sort><creationdate>20090422</creationdate><title>Crystallization and rhenium MAD phasing of the acyl-homoserinelactone synthase EsaI</title><author>Watson, W.T. ; Murphy IV, Frank V. ; Gould, Ty A. ; Jambeck, Per ; Val, Dale L. ; Cronan, Jr., John E. ; Beck von Bodman, Susan ; Churchill, Mair E.A.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-osti_scitechconnect_10063743</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2009</creationdate><topic>BACTERIA</topic><topic>BASIC BIOLOGICAL SCIENCES</topic><topic>BIOLOGICAL FUNCTIONS</topic><topic>CRYSTAL STRUCTURE</topic><topic>CRYSTALLIZATION</topic><topic>GENERAL AND MISCELLANEOUS//MATHEMATICS, COMPUTING, AND INFORMATION SCIENCE</topic><topic>LACTONES</topic><topic>PERRHENATES</topic><topic>RHENIUM</topic><topic>SPACE GROUPS</topic><topic>VIRULENCE</topic><topic>X-RAY DIFFRACTION</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Watson, W.T.</creatorcontrib><creatorcontrib>Murphy IV, Frank V.</creatorcontrib><creatorcontrib>Gould, Ty A.</creatorcontrib><creatorcontrib>Jambeck, Per</creatorcontrib><creatorcontrib>Val, Dale L.</creatorcontrib><creatorcontrib>Cronan, Jr., John E.</creatorcontrib><creatorcontrib>Beck von Bodman, Susan</creatorcontrib><creatorcontrib>Churchill, Mair E.A.</creatorcontrib><creatorcontrib>Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)</creatorcontrib><collection>OSTI.GOV</collection><jtitle>Acta crystallographica. Section D, Biological crystallography.</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Watson, W.T.</au><au>Murphy IV, Frank V.</au><au>Gould, Ty A.</au><au>Jambeck, Per</au><au>Val, Dale L.</au><au>Cronan, Jr., John E.</au><au>Beck von Bodman, Susan</au><au>Churchill, Mair E.A.</au><aucorp>Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)</aucorp><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Crystallization and rhenium MAD phasing of the acyl-homoserinelactone synthase EsaI</atitle><jtitle>Acta crystallographica. Section D, Biological crystallography.</jtitle><date>2009-04-22</date><risdate>2009</risdate><volume>57</volume><issue>2001</issue><issn>0907-4449</issn><eissn>1399-0047</eissn><abstract>Acyl-homoserine-L-lactones (AHLs) are diffusible chemical signals that are required for virulence of many Gram-negative bacteria. AHLs are produced by AHL synthases from two substrates, S-adenosyl-L-methionine and acyl-acyl carrier protein. The AHL synthase EsaI, which is homologous to the AHL synthases from other pathogenic bacterial species, has been crystallized in the primitive tetragonal space group P4{sub 3}, with unit-cell parameters a = b = 66.40, c = 47.33 {angstrom}. The structure was solved by multiple-wavelength anomalous diffraction with a novel use of the rhenium anomalous signal. The rhenium-containing structure has been refined to a resolution of 2.5 {angstrom} and the perrhenate ion binding sites and liganding residues have been identified.</abstract><cop>United States</cop></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0907-4449 |
| ispartof | Acta crystallographica. Section D, Biological crystallography., 2009-04, Vol.57 (2001) |
| issn | 0907-4449 1399-0047 |
| language | eng |
| recordid | cdi_osti_scitechconnect_1006374 |
| source | Wiley-Blackwell Read & Publish Collection; Alma/SFX Local Collection |
| subjects | BACTERIA BASIC BIOLOGICAL SCIENCES BIOLOGICAL FUNCTIONS CRYSTAL STRUCTURE CRYSTALLIZATION GENERAL AND MISCELLANEOUS//MATHEMATICS, COMPUTING, AND INFORMATION SCIENCE LACTONES PERRHENATES RHENIUM SPACE GROUPS VIRULENCE X-RAY DIFFRACTION |
| title | Crystallization and rhenium MAD phasing of the acyl-homoserinelactone synthase EsaI |
| url | http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-05T00%3A41%3A41IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-osti&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Crystallization%20and%20rhenium%20MAD%20phasing%20of%20the%20acyl-homoserinelactone%20synthase%20EsaI&rft.jtitle=Acta%20crystallographica.%20Section%20D,%20Biological%20crystallography.&rft.au=Watson,%20W.T.&rft.aucorp=Argonne%20National%20Lab.%20(ANL),%20Argonne,%20IL%20(United%20States).%20Advanced%20Photon%20Source%20(APS)&rft.date=2009-04-22&rft.volume=57&rft.issue=2001&rft.issn=0907-4449&rft.eissn=1399-0047&rft_id=info:doi/&rft_dat=%3Costi%3E1006374%3C/osti%3E%3Cgrp_id%3Ecdi_FETCH-osti_scitechconnect_10063743%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_id=info:pmid/&rfr_iscdi=true |