2olu
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 2olu |SIZE=350|CAPTION= <scene name='initialview01'>2olu</scene>, resolution 2.900Å | |PDB= 2olu |SIZE=350|CAPTION= <scene name='initialview01'>2olu</scene>, resolution 2.900Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene> | + | |LIGAND= <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= pbp2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1280 Staphylococcus aureus]) | |GENE= pbp2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1280 Staphylococcus aureus]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[2olv|2OLV]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2olu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2olu OCA], [http://www.ebi.ac.uk/pdbsum/2olu PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2olu RCSB]</span> | ||
}} | }} | ||
| Line 26: | Line 29: | ||
[[Category: Lovering, A L.]] | [[Category: Lovering, A L.]] | ||
[[Category: Strynadka, N C.]] | [[Category: Strynadka, N C.]] | ||
| - | [[Category: EDO]] | ||
[[Category: lysozyme fold]] | [[Category: lysozyme fold]] | ||
[[Category: transpeptidase fold glycosyltransferase family 51]] | [[Category: transpeptidase fold glycosyltransferase family 51]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:19:48 2008'' |
Revision as of 01:19, 31 March 2008
| |||||||
| , resolution 2.900Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Gene: | pbp2 (Staphylococcus aureus) | ||||||
| Related: | 2OLV
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 Mon Mar 31 04:19:48 2008
