3n0m | pdb_00003n0m
Crystal structure of BA2930 mutant (H183G) in complex with AcCoA
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedFor the last decade, worldwide efforts for the treatment of anthrax infection have focused on developing effective vaccines. Patients that are already infected are still treated traditionally using different types of standard antimicrobial agents. The most popular are antibiotics such as tetracyclines and fluoroquinolones. While aminoglycosides appear to be less effective antimicrobial agents than other antibiotics, synthetic aminoglycosides have been shown to act as potent inhibitors of anthrax lethal factor and may have potential application as antitoxins. Here, we present a structural analysis of the BA2930 protein, a putative aminoglycoside acetyltransferase, which may be a component of the bacterium's aminoglycoside resistance mechanism. The determined structures revealed details of a fold characteristic only for one other protein structure in the Protein Data Bank, namely, YokD from Bacillus subtilis. Both BA2930 and YokD are members of the Antibiotic_NAT superfamily (PF02522). Sequential and structural analyses showed that residues conserved throughout the Antibiotic_NAT superfamily are responsible for the binding of the cofactor acetyl coenzyme A. The interaction of BA2930 with cofactors was characterized by both crystallographic and binding studies. Structural Analysis of a Putative Aminoglycoside N-Acetyltransferase from Bacillus anthracis.,Klimecka MM, Chruszcz M, Font J, Skarina T, Shumilin I, Onopryienko O, Porebski PJ, Cymborowski M, Zimmerman MD, Hasseman J, Glomski IJ, Lebioda L, Savchenko A, Edwards A, Minor W J Mol Biol. 2011 Jul 15;410(3):411-23. Epub 2011 May 13. PMID:21601576[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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