2dln
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(New page: 200px<br /><applet load="2dln" size="450" color="white" frame="true" align="right" spinBox="true" caption="2dln, resolution 2.3Å" /> '''VANCOMYCIN RESISTANCE...)
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Revision as of 07:32, 21 November 2007
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VANCOMYCIN RESISTANCE: STRUCTURE OF D-ALANINE:D-ALANINE LIGASE AT 2.3 ANGSTROMS RESOLUTION
Overview
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.
About this Structure
2DLN is a Single protein structure of sequence from Escherichia coli with MG, ADP and PHY as ligands. Active as D-alanine--D-alanine ligase, with EC number 6.3.2.4 Full crystallographic information is available from OCA.
Reference
Vancomycin resistance: structure of D-alanine:D-alanine ligase at 2.3 A resolution., Fan C, Moews PC, Walsh CT, Knox JR, Science. 1994 Oct 21;266(5184):439-43. PMID:7939684
Page seeded by OCA on Wed Nov 21 09:39:28 2007
