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PDBsum entry 2dln

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Ligase(peptidoglycan synthesis) PDB id
2dln
Contents
Protein chain
306 a.a.
Ligands
ADP
PHY
Metals
_MG ×2
Waters ×292

References listed in PDB file
Key reference
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
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.
PROCHECK
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