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PDBsum entry 1iov

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Ligase PDB id
1iov
Jmol
Contents
Protein chain
306 a.a.
Ligands
ADP
POB
Metals
_MG ×3
Waters ×263

References listed in PDB file
Key reference
Title D-Alanine:d-Alanine ligase: phosphonate and phosphinate intermediates with wild type and the y216f mutant.
Authors C.Fan, I.S.Park, C.T.Walsh, J.R.Knox.
Ref. Biochemistry, 1997, 36, 2531-2538. [DOI no: 10.1021/bi962431t]
PubMed id 9054558
Abstract
The crystallographic structure of the D-alanine:D-alanine ligase of the ddlB gene of Escherichia coli complexed with a D-Ala-D-alpha-hydroxybutyrate phosphonate and the structure of the Y216F mutant ligase complexed with a D-Ala-D-Ala phosphinate have been determined to 2.2 and 1.9 A resolution, respectively, and refined to R factors of 0.156 and 0.158. In each complex the inhibitor has reacted with ATP to produce ADP and a tight-binding phosphorylated transition state intermediate. Comparison of these two structures with the known crystal structure of the phosphinate intermediate of the wild-type ligase shows no major conformational changes, but B factors indicate differences in mobility of loops covering the binding site. The weaker inhibition of the Y216F mutant by both inhibitors is thought to be due in part to the loss of an interloop hydrogen bond. A similar mechanism may account for poor inhibition of VanA, the homologous D-Ala:D-lactate ligase produced by vancomycin-resistant enterococci.
Secondary reference #1
Title A common fold for peptide synthetases cleaving atp to adp: glutathione synthetase and d-Alanine:d-Alanine ligase of escherichia coli.
Authors C.Fan, P.C.Moews, Y.Shi, C.T.Walsh, J.R.Knox.
Ref. Proc Natl Acad Sci U S A, 1995, 92, 1172-1176. [DOI no: 10.1073/pnas.92.4.1172]
PubMed id 7862655
Full text Abstract
Secondary reference #2
Title Vancomycin resistance: structure of d-Alanine:d-Alanine ligase at 2.3 a resolution.
Authors C.Fan, P.C.Moews, C.T.Walsh, J.R.Knox.
Ref. Science, 1994, 266, 439-443. [DOI no: 10.1126/science.7939684]
PubMed id 7939684
Full text Abstract
PROCHECK
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