2DLN

VANCOMYCIN RESISTANCE: STRUCTURE OF D-ALANINE:D-ALANINE LIGASE AT 2.3 ANGSTROMS RESOLUTION

Summary for 2DLN

• Entry DOI: 10.2210/pdb2dln/pdb
• Descriptor: D-ALANINE--D-ALANINE LIGASE, MAGNESIUM ION, ADENOSINE-5'-DIPHOSPHATE, ... (5 entities in total)
• Functional Keywords: ligase(peptidoglycan synthesis)
• Biological source: Escherichia coli
• Total number of polymer chains: 1
• Total formula weight: 33618.54

Authors

Knox, J.R.,Moews, P.C.,Fan, C. (deposition date: 1994-07-18, release date: 1995-11-01, Last modification date: 2024-02-14)

Primary citation

Fan, C.,Moews, P.C.,Walsh, C.T.,Knox, J.R.
Vancomycin resistance: structure of D-alanine:D-alanine ligase at 2.3 A resolution.
Science, 266:439-443, 1994

PubMed 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.

PubMed: 7939684

Experimental method

X-RAY DIFFRACTION (2.3 Å)