Source:http://linkedlifedata.com/resource/pubmed/id/18061205
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
3
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| pubmed:dateCreated |
2007-12-25
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| pubmed:abstractText |
The crystal structures of the universally widespread metallo-beta-lactamase (MBL) Verona integron-encoded MBL (VIM)-2 from Pseudomonas aeruginosa have been solved in their native form as well as in an unexpected oxidised form. This carbapenem-hydrolysing enzyme belongs to the so-called B1 subfamily of MBLs and shares the folding of alpha beta/beta alpha sandwich, consisting of a core of beta-sheet surrounded by alpha-helices. Surprisingly, it showed a high tendency to be strongly oxidised at the catalytic cysteine located in the Cys site, Cys221, which, in the oxidised structure, becomes a cysteinesulfonic residue. Its native structure was obtained only in the presence of Tris(2-carboxyethyl)phosphine. This oxidation might be a consequence of a lower affinity for the second Zn located in the Cys site that would also explain the observed susceptibility of VIM-2 to chelating agents. This modification, if present in nature, might play a role in catalytic down-regulation. Comparison between native and oxidised VIM-2 and a predicted model of VIM-1 (which shows one residue different in the Cys site compared with VIM-2) is performed to explain the different activities and antibiotic specificities.
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| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Asparagine,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cysteine,
http://linkedlifedata.com/resource/pubmed/chemical/Histidine,
http://linkedlifedata.com/resource/pubmed/chemical/Zinc,
http://linkedlifedata.com/resource/pubmed/chemical/beta-Lactamases
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| pubmed:status |
MEDLINE
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| pubmed:month |
Jan
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| pubmed:issn |
1089-8638
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| pubmed:author | |
| pubmed:issnType |
Electronic
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| pubmed:day |
18
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| pubmed:volume |
375
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
604-11
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| pubmed:dateRevised |
2010-11-18
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| pubmed:meshHeading |
pubmed-meshheading:18061205-Amino Acid Sequence,
pubmed-meshheading:18061205-Asparagine,
pubmed-meshheading:18061205-Bacterial Proteins,
pubmed-meshheading:18061205-Binding Sites,
pubmed-meshheading:18061205-Conserved Sequence,
pubmed-meshheading:18061205-Cysteine,
pubmed-meshheading:18061205-Escherichia coli,
pubmed-meshheading:18061205-Histidine,
pubmed-meshheading:18061205-Hydrophobic and Hydrophilic Interactions,
pubmed-meshheading:18061205-Models, Chemical,
pubmed-meshheading:18061205-Models, Molecular,
pubmed-meshheading:18061205-Molecular Sequence Data,
pubmed-meshheading:18061205-Molecular Weight,
pubmed-meshheading:18061205-Oxidation-Reduction,
pubmed-meshheading:18061205-Protein Binding,
pubmed-meshheading:18061205-Protein Conformation,
pubmed-meshheading:18061205-Protein Folding,
pubmed-meshheading:18061205-Protein Structure, Secondary,
pubmed-meshheading:18061205-Pseudomonas aeruginosa,
pubmed-meshheading:18061205-Sequence Homology, Amino Acid,
pubmed-meshheading:18061205-Substrate Specificity,
pubmed-meshheading:18061205-Zinc,
pubmed-meshheading:18061205-beta-Lactamases
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| pubmed:year |
2008
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| pubmed:articleTitle |
The three-dimensional structure of VIM-2, a Zn-beta-lactamase from Pseudomonas aeruginosa in its reduced and oxidised form.
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| pubmed:affiliation |
Laboratoire de Cristallographie Macromoléculaire, Institut de Biologie Structurale Jean-Pierre Ebel, CNRS-Commissariat à l'Energie Atomique (CEA)-Université Joseph Fourier, 41 rue Jules Horowitz, F-38027 Grenoble Cedex 1, France. isabel.garcia@ibs.fr
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| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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