1w4t

X-ray crystallographic structure of Pseudomonas aeruginosa arylamine N-acetyltransferaseX-ray crystallographic structure of Pseudomonas aeruginosa arylamine N-acetyltransferase

Structural highlights 1w4t is a 1 chain structure with sequence from Pseudomonas aeruginosa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.95Å Ligands: Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q9HUY3_PSEAE 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 The gene for NAT (arylamine N-acetyltransferase) from Pseudomonas aeruginosa (panat) has been cloned from genomic DNA, and the gene product (PANAT) expressed as an N-terminal histidine-tagged protein in Escherichia coli and purified via nickel ion affinity chromatography. The specific activities of PANAT against a broad range of substrates have been investigated and compared with those of other prokaryotic NAT enzymes. For most arylamine substrates identified, PANAT exhibits in vitro specific activities typically one order of magnitude greater than those of recombinant NAT enzymes from Mycobacterium smegmatis or Salmonella typhimurium. Among the substrates of PANAT so far identified are the anti-tubercular drug isoniazid, 5-aminosalicylate (a drug used in the treatment of inflammatory bowel disease), as well as important environmental pollutants such as 3,4-dichloroaniline and 2-aminofluorene. As well as acetylating common NAT substrates, PANAT is unique among the prokaryotic NATs so far studied in acetylating the folate precursor 4-aminobenzoic acid and the folate catabolite 4-aminobenzoylglutamate. The recombinant protein has been expressed in sufficient quantity to allow protein crystallization, and we have subsequently determined the 1.95 A structure of PANAT by X-ray crystallography. Expression, purification, characterization and structure of Pseudomonas aeruginosa arylamine N-acetyltransferase.,Westwood IM, Holton SJ, Rodrigues-Lima F, Dupret JM, Bhakta S, Noble ME, Sim E Biochem J. 2005 Jan 15;385(Pt 2):605-12. PMID:15447630 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Arylamine N-acetyltransferase 3D structures

spinqualitylabelsall models 1w4t, resolution 1.95Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image