4wbg
From Proteopedia
(Difference between revisions)
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- | ''' | + | ==Crystal structure of class C beta-lactamase Mox-1 covalently complexed with aztorenam== |
+ | <StructureSection load='4wbg' size='340' side='right' caption='[[4wbg]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[4wbg]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WBG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4WBG FirstGlance]. <br> | ||
+ | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=AZR:2-({[(1Z)-1-(2-AMINO-1,3-THIAZOL-4-YL)-2-OXO-2-{[(2S,3S)-1-OXO-3-(SULFOAMINO)BUTAN-2-YL]AMINO}ETHYLIDENE]AMINO}OXY)-2-METHYLPROPANOIC+ACID'>AZR</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | ||
+ | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3w8k|3w8k]]</td></tr> | ||
+ | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-lactamase Beta-lactamase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.2.6 3.5.2.6] </span></td></tr> | ||
+ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4wbg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wbg OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4wbg RCSB], [http://www.ebi.ac.uk/pdbsum/4wbg PDBsum]</span></td></tr> | ||
+ | </table> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | We solved the crystal structure of a class C beta-lactamase MOX-1 complexed with an inhibitor, aztreonam, at 1.9A resolution. The main-chain oxygen of Ser315 interacts with the amide nitrogen of aztreonam. Surprisingly, compared to the free MOX-1 structure, this main-chain carboxyl changes its position significantly upon binding aztreonam. This result indicates that the interaction between MOX-1 and beta-lactams can be accompanied by conformational changes of the B3 beta-strand main chain. | ||
- | + | A Conformational Change Observed in the Active Site of Class C beta-Lactamase MOX-1 in Binding Aztreonam.,Oguri T, Ishii Y, Shimizu-Ibuka A Antimicrob Agents Chemother. 2015 Jun 8. pii: AAC.04428-14. PMID:26055361<ref>PMID:26055361</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
- | + | == References == | |
- | [[Category: | + | <references/> |
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Beta-lactamase]] | ||
+ | [[Category: Ishii, Y]] | ||
[[Category: Oguri, T]] | [[Category: Oguri, T]] | ||
- | [[Category: | + | [[Category: Shimizu-ibuka, A]] |
- | [[Category: | + | [[Category: Acyl-intermediate]] |
+ | [[Category: Aztreonam]] | ||
+ | [[Category: Hydrolase]] |
Revision as of 12:08, 1 July 2015
Crystal structure of class C beta-lactamase Mox-1 covalently complexed with aztorenam
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