 |
PDBsum entry 2dln
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
|
|
|
|
|
|
|
|
|
|
Ligase(peptidoglycan synthesis)
|
PDB id
|
|
|
|
2dln
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
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: ]
|
 |
|
PubMed id
|
 |
|
 |
 |
|
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.
|
 |
|
|
|
|
 |