2olu
From Proteopedia
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[[Image:2olu.gif|left|200px]] | [[Image:2olu.gif|left|200px]] | ||
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'''Structural Insight Into the Transglycosylation Step Of Bacterial Cell Wall Biosynthesis : Apoenzyme''' | '''Structural Insight Into the Transglycosylation Step Of Bacterial Cell Wall Biosynthesis : Apoenzyme''' | ||
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[[Category: Lovering, A L.]] | [[Category: Lovering, A L.]] | ||
[[Category: Strynadka, N C.]] | [[Category: Strynadka, N C.]] | ||
| - | [[Category: | + | [[Category: Lysozyme fold]] |
| - | [[Category: | + | [[Category: Transpeptidase fold glycosyltransferase family 51]] |
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Revision as of 08:10, 4 May 2008
Structural Insight Into the Transglycosylation Step Of Bacterial Cell Wall Biosynthesis : Apoenzyme
Overview
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.
About this Structure
2OLU is a Single protein structure of sequence from Staphylococcus aureus. Full crystallographic information is available from OCA.
Reference
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 Page seeded by OCA on Sun May 4 11:10:56 2008
