2oqo
From Proteopedia
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|PDB= 2oqo |SIZE=350|CAPTION= <scene name='initialview01'>2oqo</scene>, resolution 2.10Å | |PDB= 2oqo |SIZE=350|CAPTION= <scene name='initialview01'>2oqo</scene>, resolution 2.10Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=CPS:3-[(3-CHOLAMIDOPROPYL)DIMETHYLAMMONIO]-1-PROPANESULFONATE'>CPS</scene>, <scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= mrcA, ponA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=63363 Aquifex aeolicus]) | |GENE= mrcA, ponA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=63363 Aquifex aeolicus]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2oqo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2oqo OCA], [http://www.ebi.ac.uk/pdbsum/2oqo PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2oqo RCSB]</span> | ||
}} | }} | ||
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[[Category: Walker, S.]] | [[Category: Walker, S.]] | ||
[[Category: Yuan, Y.]] | [[Category: Yuan, Y.]] | ||
| - | [[Category: CPS]] | ||
| - | [[Category: EPE]] | ||
[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''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 04:21:43 2008'' |
Revision as of 01:21, 31 March 2008
| |||||||
| , resolution 2.10Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Gene: | mrcA, ponA (Aquifex aeolicus) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of a peptidoglycan glycosyltransferase from a class A PBP: insight into bacterial cell wall synthesis
Overview
Peptidoglycan is an essential polymer that forms a protective shell around bacterial cell membranes. Peptidoglycan biosynthesis is the target of many clinically used antibiotics, including the beta-lactams, imipenems, cephalosporins, and glycopeptides. Resistance to these and other antibiotics has prompted interest in an atomic-level understanding of the enzymes that make peptidoglycan. Representative structures have been reported for most of the enzymes in the pathway. Until now, however, there have been no structures of any peptidoglycan glycosyltransferases (also known as transglycosylases), which catalyze formation of the carbohydrate chains of peptidoglycan from disaccharide subunits on the bacterial cell surface. We report here the 2.1-A crystal structure of the peptidoglycan glycosyltransferase (PGT) domain of Aquifex aeolicus PBP1A. The structure has a different fold from all other glycosyltransferase structures reported to date, but it bears some resemblance to lambda-lysozyme, an enzyme that degrades the carbohydrate chains of peptidoglycan. An analysis of the structure, combined with biochemical information showing that these enzymes are processive, suggests a model for glycan chain polymerization.
About this Structure
2OQO is a Single protein structure of sequence from Aquifex aeolicus. Full crystallographic information is available from OCA.
Reference
Crystal structure of a peptidoglycan glycosyltransferase suggests a model for processive glycan chain synthesis., Yuan Y, Barrett D, Zhang Y, Kahne D, Sliz P, Walker S, Proc Natl Acad Sci U S A. 2007 Mar 27;104(13):5348-53. Epub 2007 Mar 8. PMID:17360321
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