PMID:7939684
| Citation |
Fan, C, Moews, PC, Walsh, CT and Knox, JR (1994) Vancomycin resistance: structure of D-alanine:D-alanine ligase at 2.3 A resolution. Science 266:439-43 |
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| Abstract |
The molecular structure of the D-alanine:D-alanine ligase of the ddlB gene of Escherichia coli, co-crystallized with an S,R-methylphosphinate and adenosine triphosphate, was determined by x-ray diffraction to a resolution of 2.3 angstroms. A catalytic mechanism for the ligation of two D-alanine substrates is proposed in which a helix dipole and a hydrogen-bonded triad of tyrosine, serine, and glutamic acid assist binding and deprotonation steps. From sequence comparison, it is proposed that a different triad exists in a recently discovered D-alanine:D-lactate ligase (VanA) present in vancomycin-resistant enterococci. A molecular mechanism for the altered specificity of VanA is suggested. |
| Links | |
| Keywords |
Adenosine Diphosphate/chemistry; Adenosine Diphosphate/metabolism; Amino Acid Sequence; Bacterial Proteins/chemistry; Binding Sites; Carbon-Oxygen Ligases; Computer Graphics; Crystallography, X-Ray; Dipeptides/biosynthesis; Drug Resistance, Microbial; Escherichia coli/drug effects; Escherichia coli/enzymology; Hydrogen Bonding; Ligases/chemistry; Models, Molecular; Molecular Sequence Data; Molecular Structure; Peptide Synthases/chemistry; Peptide Synthases/genetics; Peptide Synthases/metabolism; Protein Structure, Secondary; Protein Structure, Tertiary; Substrate Specificity; Vancomycin/pharmacology |
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