5ctn: Difference between revisions
New page: '''Unreleased structure''' The entry 5ctn is ON HOLD Authors: Smith, C.A., Vakulenko, S.B. Description: Structure of BPu1 beta-lactamase Category: Unreleased Structures [[Category:... |
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==Structure of BPu1 beta-lactamase== | |||
<StructureSection load='5ctn' size='340' side='right'caption='[[5ctn]], [[Resolution|resolution]] 1.35Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5ctn]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_pumilus Bacillus pumilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CTN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5CTN FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.35Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=5R7:(2~{S},3~{R})-3-METHYL-2-[(2~{S},3~{R})-3-OXIDANYL-1-OXIDANYLIDENE-BUTAN-2-YL]-4-[(3~{S},5~{S})-5-[(SULFAMOYLAMINO)METHYL]PYRROLIDIN-3-YL]SULFANYL-3,4-DIHYDRO-2~{H}-PYRROLE-5-CARBOXYLIC+ACID'>5R7</scene>, <scene name='pdbligand=FLC:CITRATE+ANION'>FLC</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5ctn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ctn OCA], [https://pdbe.org/5ctn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ctn RCSB], [https://www.ebi.ac.uk/pdbsum/5ctn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ctn ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/A8FFI9_BACP2 A8FFI9_BACP2] | |||
<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> | |||
[[Category: | </div> | ||
[[Category: Smith | <div class="pdbe-citations 5ctn" style="background-color:#fffaf0;"></div> | ||
[[Category: Vakulenko | |||
==See Also== | |||
*[[Beta-lactamase 3D structures|Beta-lactamase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Bacillus pumilus]] | |||
[[Category: Large Structures]] | |||
[[Category: Smith CA]] | |||
[[Category: Vakulenko SB]] | |||
Latest revision as of 10:03, 17 October 2024
Structure of BPu1 beta-lactamaseStructure of BPu1 beta-lactamase
Structural highlights
FunctionPublication Abstract from PubMedProduction 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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