1e4e

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{{STRUCTURE_1e4e| PDB=1e4e | SCENE= }}
{{STRUCTURE_1e4e| PDB=1e4e | SCENE= }}
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'''D-ALANYL-D-LACATE LIGASE'''
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===D-ALANYL-D-LACATE LIGASE===
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==Overview==
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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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(as it appears on PubMed at http://www.pubmed.gov), where 10908650 is the PubMed ID number.
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{{ABSTRACT_PUBMED_10908650}}
==About this Structure==
==About this Structure==
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[[Category: Peptidoglycan synthesis]]
[[Category: Peptidoglycan synthesis]]
[[Category: Plasmid]]
[[Category: Plasmid]]
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Revision as of 21:07, 30 June 2008

Image:1e4e.png

Template:STRUCTURE 1e4e

D-ALANYL-D-LACATE LIGASE

Template:ABSTRACT PUBMED 10908650

About this Structure

1E4E is a Protein complex structure of sequences from Enterococcus faecium. Full crystallographic information is available from OCA.

Reference

The molecular basis of vancomycin resistance in clinically relevant Enterococci: crystal structure of D-alanyl-D-lactate ligase (VanA)., Roper DI, Huyton T, Vagin A, Dodson G, Proc Natl Acad Sci U S A. 2000 Aug 1;97(16):8921-5. PMID:10908650

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