2olv: Difference between revisions
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[[Image:2olv.jpg|left|200px]] | [[Image:2olv.jpg|left|200px]] | ||
'''Structural Insight Into the Transglycosylation Step Of Bacterial Cell Wall Biosynthesis : Donor Ligand Complex''' | {{Structure | ||
|PDB= 2olv |SIZE=350|CAPTION= <scene name='initialview01'>2olv</scene>, resolution 2.800Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=M0E:MOENOMYCIN'>M0E</scene> | |||
|ACTIVITY= | |||
|GENE= pbp2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1280 Staphylococcus aureus]) | |||
}} | |||
'''Structural Insight Into the Transglycosylation Step Of Bacterial Cell Wall Biosynthesis : Donor Ligand Complex''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2OLV is a [ | 2OLV is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OLV OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/17347437 17347437] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Staphylococcus aureus]] | [[Category: Staphylococcus aureus]] | ||
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[[Category: transpeptidase fold]] | [[Category: transpeptidase fold]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:01:23 2008'' | ||
Revision as of 19:01, 20 March 2008
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| , resolution 2.800Å | |||||||
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| Ligands: | |||||||
| Gene: | pbp2 (Staphylococcus aureus) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Structural Insight Into the Transglycosylation Step Of Bacterial Cell Wall Biosynthesis : Donor Ligand Complex
OverviewOverview
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 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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