3lnb

Crystal Structure Analysis of Arylamine N-acetyltransferase C from Bacillus anthracis

spinqualitylabelsall models 3lnb, resolution 2.01Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3lnb is a 1 chain structure with sequence from Bacillus anthracis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.01Å Ligands: COA, FMT Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A6L7HKL6_BACAN Publication Abstract from PubMed Arylamine N-acetyltransferases (NATs) are xenobiotic-metabolizing enzymes that biotransform arylamine drugs. The Bacillus anthracis (BACAN)NAT1 enzyme affords increased resistance to the antibiotic sulfamethoxazole through its acetylation. We report the structure of (BACAN)NAT1. Unexpectedly, endogenous coenzymeA was present in the active site. The structure suggests that, contrary to the other prokaryotic NATs, (BACAN)NAT1 possesses a 14-residue insertion equivalent to the "mammalian insertion", a structural feature considered unique to mammalian NATs. Moreover, (BACAN)NAT1 structure shows marked differences in the mode of binding and location of coenzymeA when compared to the other NATs. This suggests that the mechanisms of cofactor recognition by NATs is more diverse than expected and supports the cofactor-binding site as being a unique subsite to target in drug design against bacterial NATs. The Bacillus anthracis arylamine N-acetyltransferase ((BACAN)NAT1) that inactivates sulfamethoxazole, reveals unusual structural features compared with the other NAT isoenzymes.,Pluvinage B, Li de la Sierra-Gallay I, Kubiak X, Xu X, Dairou J, Dupret JM, Rodrigues-Lima F FEBS Lett. 2011 Dec 15;585(24):3947-52. Epub 2011 Nov 2. PMID:22062153 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Arylamine N-acetyltransferase 3D structures

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