2vfb | pdb_00002vfb

The structure of Mycobacterium marinum arylamine N-acetyltransferase

spinqualitylabelsall models 2vfb, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2vfb is a 1 chain structure with sequence from "mycobacterium_balnei"_linell_and_norden_1952 "mycobacterium balnei" linell and norden 1952. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 2vfc Activity: Arylamine N-acetyltransferase, with EC number 2.3.1.5 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Arylamine N-acetyltransferase (NAT) enzymes are widespread in nature. They serve to acetylate xenobiotics and/or endogenous substrates using acetyl coenzyme A (CoA) as a cofactor. Conservation of the architecture of the NAT enzyme family from mammals to bacteria has been demonstrated by a series of prokaryotic NAT structures, together with the recently reported structure of human NAT1. We report here the cloning, purification, kinetic characterisation and crystallographic structure determination of NAT from Mycobacterium marinum, a close relative of the pathogenic Mycobacterium tuberculosis. We have also determined the structure of M. marinum NAT in complex with CoA, shedding the first light on cofactor recognition in prokaryotic NATs. Surprisingly, the principal CoA recognition site in M. marinum NAT is located some 30 A from the site of CoA recognition in the recently deposited structure of human NAT2 bound to CoA. The structure explains the Ping-Pong Bi-Bi reaction mechanism of NAT enzymes and suggests mechanisms by which the acetylated enzyme intermediate may be protected. Recognition of CoA in a much wider groove in prokaryotic NATs suggests that this subfamily may accommodate larger substrates than is the case for human NATs and may assist in the identification of potential endogenous substrates. It also suggests the cofactor-binding site as a unique subsite to target in drug design directed against NAT in mycobacteria. Divergence of cofactor recognition across evolution: coenzyme A binding in a prokaryotic arylamine N-acetyltransferase.,Fullam E, Westwood IM, Anderton MC, Lowe ED, Sim E, Noble ME J Mol Biol. 2008 Jan 4;375(1):178-91. Epub 2007 Oct 13. PMID:18005984 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Arylamine N-acetyltransferase 3D structures

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