2olv

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(New page: 200px<br /><applet load="2olv" size="350" color="white" frame="true" align="right" spinBox="true" caption="2olv, resolution 2.800&Aring;" /> '''Structural Insight ...)
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==Overview==
==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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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==
==About this Structure==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Staphylococcus aureus]]
[[Category: Staphylococcus aureus]]
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[[Category: Castro, L.De.]]
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[[Category: Castro, L De.]]
[[Category: Lim, D.]]
[[Category: Lim, D.]]
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[[Category: Lovering, A.L.]]
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[[Category: Lovering, A L.]]
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[[Category: Strynadka, N.C.J.]]
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[[Category: Strynadka, N C.J.]]
[[Category: M0E]]
[[Category: M0E]]
[[Category: glycosyltransferase family 51]]
[[Category: glycosyltransferase family 51]]
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[[Category: transpeptidase fold]]
[[Category: transpeptidase fold]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jan 29 21:13:10 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:19:56 2008''

Revision as of 16:20, 21 February 2008


2olv, resolution 2.800Å

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

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

2OLV is a Single protein structure of sequence from Staphylococcus aureus with as ligand. 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

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