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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
16
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pubmed:dateCreated |
2000-9-5
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pubmed:databankReference |
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pubmed:abstractText |
d-alanine-d-lactate ligase from Enterococcus faecium BM4147 is directly responsible for the biosynthesis of alternate cell-wall precursors in bacteria, which are resistant to the glycopeptide antibiotic vancomycin. The crystal structure has been determined with data extending to 2.5-A resolution. This structure shows that the active site has unexpected interactions and is distinct from previous models for d-alanyl-d-lactate ligase mechanistic studies. It appears that the preference of the enzyme for lactate as a ligand over d-alanine could be mediated by electrostatic effects and/or a hydrogen-bonding network, which principally involve His-244. The structure of d-alanyl-d-lactate ligase provides a revised interpretation of the molecular events that lead to vancomycin resistance.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/10908650-10417422,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10908650-10529248,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10908650-10801495,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10908650-15299926,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10908650-1551598,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10908650-1931965,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10908650-7854121,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10908650-7862655,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10908650-7893688,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10908650-7939684,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10908650-8564538,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10908650-8631706,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10908650-8756703,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10908650-8807824,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10908650-8807826,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10908650-8989312,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10908650-9054558,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10908650-9083053,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10908650-9294159,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10908650-9416615,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10908650-9761844
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0027-8424
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
97
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
8921-5
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
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pubmed:year |
2000
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pubmed:articleTitle |
The molecular basis of vancomycin resistance in clinically relevant Enterococci: crystal structure of D-alanyl-D-lactate ligase (VanA).
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pubmed:affiliation |
York Structural Biology Laboratory, Department of Chemistry, The University of York, Heslington, York YO10 5DD, United Kingdom. roper@ysbl.york.ac.uk
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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