5ctm: Difference between revisions
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''' | ==Structure of BPu1 beta-lactamase== | ||
<StructureSection load='5ctm' size='340' side='right' caption='[[5ctm]], [[Resolution|resolution]] 1.00Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5ctm]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CTM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5CTM FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FLC:CITRATE+ANION'>FLC</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr> | |||
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=KCX:LYSINE+NZ-CARBOXYLIC+ACID'>KCX</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5ctn|5ctn]]</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=5ctm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ctm OCA], [http://pdbe.org/5ctm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ctm RCSB], [http://www.ebi.ac.uk/pdbsum/5ctm PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Production of beta-lactamases of one of four molecular classes (A, B, C and D) is the major mechanism of bacterial resistance to beta-lactams, the largest class of antibiotics, which have saved countless lives since their inception 70 years ago. Although several hundred efficient class D enzymes have been identified in Gram-negative pathogens over the last four decades, none have been reported in Gram-positive bacteria. Here we demonstrate that efficient class D beta-lactamases capable of hydrolyzing a wide array of beta-lactam substrates are widely disseminated in various species of environmental Gram-positive organisms. Class D enzymes of Gram-positive bacteria have a distinct structural architecture and employ a unique substrate-binding mode that is quite different from that of all currently known class A, C and D beta-lactamases. These enzymes thus constitute a previously unknown reservoir of novel antibiotic-resistance enzymes. | |||
Class D beta-lactamases do exist in Gram-positive bacteria.,Toth M, Antunes NT, Stewart NK, Frase H, Bhattacharya M, Smith CA, Vakulenko SB Nat Chem Biol. 2015 Nov 9. doi: 10.1038/nchembio.1950. PMID:26551395<ref>PMID:26551395</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 5ctm" style="background-color:#fffaf0;"></div> | |||
[[Category: | == References == | ||
[[Category: Smith, C | <references/> | ||
[[Category: Vakulenko, S | __TOC__ | ||
</StructureSection> | |||
[[Category: Beta-lactamase]] | |||
[[Category: Smith, C A]] | |||
[[Category: Vakulenko, S B]] | |||
[[Category: Hydrolase]] | |||
