2olv: Difference between revisions

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{{STRUCTURE_2olv|  PDB=2olv  |  SCENE=  }}  
{{STRUCTURE_2olv|  PDB=2olv  |  SCENE=  }}  


'''Structural Insight Into the Transglycosylation Step Of Bacterial Cell Wall Biosynthesis : Donor Ligand Complex'''
===Structural Insight Into the Transglycosylation Step Of Bacterial Cell Wall Biosynthesis : Donor Ligand Complex===




==Overview==
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Peptidoglycan glycosyltransferases (GTs) catalyze the polymerization step of cell-wall biosynthesis, are membrane-bound, and are highly conserved across all bacteria. Long considered the "holy grail" of antibiotic research, they represent an essential and easily accessible drug target for antibiotic-resistant bacteria, including methicillin-resistant Staphylococcus aureus. We have determined the 2.8 angstrom structure of a bifunctional cell-wall cross-linking enzyme, including its transpeptidase and GT domains, both unliganded and complexed with the substrate analog moenomycin. The peptidoglycan GTs adopt a fold distinct from those of other GT classes. The structures give insight into critical features of the catalytic mechanism and key interactions required for enzyme inhibition.
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{{ABSTRACT_PUBMED_17347437}}


==About this Structure==
==About this Structure==
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[[Category: Lysozyme fold]]
[[Category: Lysozyme fold]]
[[Category: Transpeptidase fold]]
[[Category: Transpeptidase fold]]
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Revision as of 23:41, 27 July 2008

File:2olv.png

Template:STRUCTURE 2olv

Structural Insight Into the Transglycosylation Step Of Bacterial Cell Wall Biosynthesis : Donor Ligand ComplexStructural Insight Into the Transglycosylation Step Of Bacterial Cell Wall Biosynthesis : Donor Ligand Complex

Template:ABSTRACT PUBMED 17347437

About this StructureAbout this Structure

2OLV is a Single protein structure of sequence from Staphylococcus aureus. Full crystallographic information is available from OCA.

ReferenceReference

Structural insight into the transglycosylation step of bacterial cell-wall biosynthesis., Lovering AL, de Castro LH, Lim D, Strynadka NC, Science. 2007 Mar 9;315(5817):1402-5. PMID:17347437

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