1khr: Difference between revisions
No edit summary |
No edit summary |
||
| Line 4: | Line 4: | ||
|PDB= 1khr |SIZE=350|CAPTION= <scene name='initialview01'>1khr</scene>, resolution 2.8Å | |PDB= 1khr |SIZE=350|CAPTION= <scene name='initialview01'>1khr</scene>, resolution 2.8Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=VIR:VIRGINIAMYCIN+M1'>VIR</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= satA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1352 Enterococcus faecium]) | |GENE= satA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1352 Enterococcus faecium]) | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1khr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1khr OCA], [http://www.ebi.ac.uk/pdbsum/1khr PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1khr RCSB]</span> | |||
}} | }} | ||
| Line 24: | Line 27: | ||
[[Category: Roderick, S L.]] | [[Category: Roderick, S L.]] | ||
[[Category: Sugantino, M.]] | [[Category: Sugantino, M.]] | ||
[[Category: acyltransferase]] | [[Category: acyltransferase]] | ||
[[Category: antibiotic resistance]] | [[Category: antibiotic resistance]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:48:46 2008'' | ||
Revision as of 21:48, 30 March 2008
| |||||||
| , resolution 2.8Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Gene: | satA (Enterococcus faecium) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure of Vat(D) in Complex with Virginiamycin and Coenzyme A
OverviewOverview
The streptogramin class of antibiotics act to inhibit bacterial protein synthesis, and their semisynthetic derivatives, such as dalfopristin-quinupristin (Synercid), are used to treat serious or life-threatening infections due to multiply antibiotic resistant bacteria. Acquired resistance of the nosocomial pathogen Enterococcus faecium to the group A component of natural and semisynthetic streptogramin mixtures is a prerequisite for the streptogramin resistance phenotype and is mediated by a streptogramin acetyltransferase. The crystal structure of Vat(D), a streptogramin acetyltransferase from a human urinary isolate of E. faecium, has been determined as an apoenzyme and in complex with either acetyl-CoA or virginiamycin M1 and CoA. These structures illustrate the location and arrangement of residues at the active site, and point to His 82 as a residue that may function as a general base. The structural similarity of Vat(D) to the xenobiotic acetyltransferase from Pseudomonas aeruginosa indicates similarities in the catalytic mechanism for these enzymes as well as several shared and distinctive antibiotic binding interactions between these enzymes and their respective substrates. These results reveal the molecular basis for a reaction by which Gram-positive cocci acquire resistance to a last resort antibiotic.
About this StructureAbout this Structure
1KHR is a Single protein structure of sequence from Enterococcus faecium. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of Vat(D): an acetyltransferase that inactivates streptogramin group A antibiotics., Sugantino M, Roderick SL, Biochemistry. 2002 Feb 19;41(7):2209-16. PMID:11841212
Page seeded by OCA on Sun Mar 30 21:48:46 2008