1khr

<table><tr><td colspan='2'>[[1khr]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_19434 Atcc 19434]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KHR OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1KHR FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=VIR:VIRGINIAMYCIN+M1'>VIR</scene></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">satA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1352 ATCC 19434])</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1khr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1khr OCA], [http://pdbe.org/1khr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1khr RCSB], [http://www.ebi.ac.uk/pdbsum/1khr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1khr ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/VATD_ENTFC VATD_ENTFC]] Inactivates the A compounds of streptogramin antibiotics by acetylation, thus providing resistance to these antibiotics.

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== Publication Abstract from PubMed ==

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.

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<ref>PMID:11841212</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

<references/>

[[Category: Atcc 19434]]

[[Category: Roderick, S L]]

[[Category: Sugantino, M]]

[[Category: Transferase-antibiotic complex]]