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6jv4

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Current revision (10:39, 27 March 2024) (edit) (undo)
 
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<StructureSection load='6jv4' size='340' side='right'caption='[[6jv4]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
<StructureSection load='6jv4' size='340' side='right'caption='[[6jv4]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6jv4]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"oceanomonas_alginolytica"_miyamoto_et_al._1961 "oceanomonas alginolytica" miyamoto et al. 1961]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6JV4 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6JV4 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6jv4]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Vibrio_alginolyticus Vibrio alginolyticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6JV4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6JV4 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">vmb-1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=663 "Oceanomonas alginolytica" Miyamoto et al. 1961])</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6jv4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6jv4 OCA], [http://pdbe.org/6jv4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6jv4 RCSB], [http://www.ebi.ac.uk/pdbsum/6jv4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6jv4 ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6jv4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6jv4 OCA], [https://pdbe.org/6jv4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6jv4 RCSB], [https://www.ebi.ac.uk/pdbsum/6jv4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6jv4 ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/A0A5Q5ADH9_VIBAL A0A5Q5ADH9_VIBAL]
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The increasing incidence of phenotypic resistance to carbapenems in recent years is mainly attributed to acquisition of mobile carbapenemase-encoding genetic elements by major bacterial pathogens. Here, a novel carbapenemase known as Vibrio metallo-beta-lactamase 1 (VMB-1), which is encoded by a gene (blaVMB-1 ) located in an integron-bearing, highly transmissible IncC type plasmid, namely pVB1796, is identified and characterized, both genetically and functionally. Recovered from a foodborne Vibrio alginolyticus strain that exhibits resistance to all known beta-lactam antibiotics, pVB1796 is found to possess a hybrid backbone that exhibits unique features of both type 1 and type 2 IncC elements. VMB-1 exhibits 94% sequence homology with several recently reported but poorly characterized metallo-beta-lactamases (MBLs) produced by the marine organisms Alteromonadaceae, Glaciecola, and Thalassomonas actiniarum. Sequence alignment analysis shows that VMB-1 shares a structurally identical active site with subclass B1 MBLs. Importantly, pVB1796 is found to be efficiently transferred from Vibrio to other Gram-negative bacterial pathogens, including Salmonella typhimurium, Klebsiella pneumoniae, and Acinetobacter baumanni, via conjugation. These findings suggest that blaVMB-1 -bearing plasmids have the potential to be disseminated to other Gram-negative bacterial pathogens in the near future and render carbapenems useless in treatment of multidrug resistant infections.
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Genetic and Biochemical Characterization of VMB-1, a Novel Metallo-beta-Lactamase Encoded by a Conjugative, Broad-Host Range IncC Plasmid from Vibrio spp.,Zheng Z, Cheng Q, Chan EW, Chen S Adv Biosyst. 2020 Mar;4(3):e1900221. doi: 10.1002/adbi.201900221. Epub 2020 Jan, 29. PMID:32293144<ref>PMID:32293144</ref>
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==See Also==
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*[[Beta-lactamase 3D structures|Beta-lactamase 3D structures]]
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 6jv4" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Oceanomonas alginolytica miyamoto et al. 1961]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Chen, S]]
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[[Category: Vibrio alginolyticus]]
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[[Category: Cheng, Q]]
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[[Category: Chen S]]
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[[Category: Hydrolase]]
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[[Category: Cheng Q]]
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[[Category: Metallo-beta-lactamase]]
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[[Category: Subclasse b1]]
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Current revision

Crystal structure of metallo-beta-lactamase VMB-1

PDB ID 6jv4

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