2dln: Difference between revisions

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[[Image:2dln.jpg|left|200px]]
{{Seed}}
[[Image:2dln.png|left|200px]]


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{{STRUCTURE_2dln|  PDB=2dln  |  SCENE=  }}  
{{STRUCTURE_2dln|  PDB=2dln  |  SCENE=  }}  


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




==Overview==
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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.
The line below this paragraph, {{ABSTRACT_PUBMED_7939684}}, adds the Publication Abstract to the page
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{{ABSTRACT_PUBMED_7939684}}


==About this Structure==
==About this Structure==
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[[Category: Knox, J R.]]
[[Category: Knox, J R.]]
[[Category: Moews, P C.]]
[[Category: Moews, P C.]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 00:41:19 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 15:53:59 2008''

Revision as of 12:54, 29 July 2008

File:2dln.png

Template:STRUCTURE 2dln

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

Template:ABSTRACT PUBMED 7939684

About this Structure

2DLN is a Single protein structure of sequence from Escherichia coli. 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

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