2oqw: Difference between revisions
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==The crystal structure of sortase B from B.anthracis in complex with AAEK1== | ==The crystal structure of sortase B from B.anthracis in complex with AAEK1== | ||
<StructureSection load='2oqw' size='340' side='right' caption='[[2oqw]], [[Resolution|resolution]] 2.10Å' scene=''> | <StructureSection load='2oqw' size='340' side='right'caption='[[2oqw]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2oqw]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2oqw]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_anthracis_(strain_ames) Bacillus anthracis (strain ames)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OQW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2OQW FirstGlance]. <br> | ||
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CS3:S-[3-OXO-3-(2-THIENYL)PROPYL]-L-CYSTEINE'>CS3</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CS3:S-[3-OXO-3-(2-THIENYL)PROPYL]-L-CYSTEINE'>CS3</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BA_4783, BAS4438, GBAA4783 ([ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BA_4783, BAS4438, GBAA4783 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=198094 Bacillus anthracis (strain Ames)])</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2oqw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2oqw OCA], [https://pdbe.org/2oqw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2oqw RCSB], [https://www.ebi.ac.uk/pdbsum/2oqw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2oqw ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Joachimiak, A]] | [[Category: Joachimiak, A]] | ||
[[Category: Marresso, A W]] | [[Category: Marresso, A W]] | ||
Revision as of 16:03, 9 June 2021
The crystal structure of sortase B from B.anthracis in complex with AAEK1The crystal structure of sortase B from B.anthracis in complex with AAEK1
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedSortases anchor surface proteins to the cell wall of Gram-positive pathogens through recognition of specific motif sequences. Loss of sortase leads to large reductions in virulence, which identifies sortase as a target for the development of antibacterials. By screening 135,625 small molecules for inhibition, we report here that aryl (beta-amino)ethyl ketones inhibit sortase enzymes from staphylococci and bacilli. Inhibition of sortases occurs through an irreversible, covalent modification of their active site cysteine. Sortases specifically activate this class of molecules via beta-elimination, generating a reactive olefin intermediate that covalently modifies the cysteine thiol. Analysis of the three-dimensional structure of Bacillus anthracis sortase B with and without inhibitor provides insights into the mechanism of inhibition and reveals binding pockets that can be exploited for drug discovery. Activation of inhibitors by sortase triggers irreversible modification of the active site.,Maresso AW, Wu R, Kern JW, Zhang R, Janik D, Missiakas DM, Duban ME, Joachimiak A, Schneewind O J Biol Chem. 2007 Aug 10;282(32):23129-39. Epub 2007 Jun 1. PMID:17545669[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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