2bsz
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(New page: 200px<br /><applet load="2bsz" size="350" color="white" frame="true" align="right" spinBox="true" caption="2bsz, resolution 2.00Å" /> '''STRUCTURE OF MESORHI...)
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Revision as of 16:30, 29 January 2008
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STRUCTURE OF MESORHIZOBIUM LOTI ARYLAMINE N-ACETYLTRANSFERASE 1
Overview
The arylamine N-acetyltransferase (NAT) enzymes have been found in a broad, range of both eukaryotic and prokaryotic organisms. The NAT enzymes, catalyse the transfer of an acetyl group from acetyl Co-enzyme A onto the, terminal nitrogen of a range of arylamine, hydrazine and arylhydrazine, compounds. Recently, several NAT structures have been reported from, different prokaryotic sources including Salmonella typhimurium, Mycobacterium smegmatis and Pseudomonas aeruginosa. Bioinformatics, analysis of the Mesorhizobium loti genome revealed two NAT paralogues, the, first example of multiple NAT isoenzymes in a eubacterial organism. The M., loti NAT 1 enzyme was recombinantly expressed and purified for X-ray, crystallographic studies. The purified enzyme was crystallized in 0.5 M, Ca(OAc)2, 16% PEG 3350, 0.1 M Tris-HCl pH 8.5 using the sitting-drop, vapour-diffusion method. A data set diffracting to 2.0 A was collected, from a single crystal at 100 K. The crystal belongs to the orthorhombic, spacegroup P2(1)2(1)2(1), with unit-cell parameters a = 53.2, b = 97.3, c, = 114.3 A. The structure was refined to a final free-R factor of 24.8%., The structure reveals that despite low sequence homology, M. loti NAT1, shares the common fold as reported in previous NAT structures and exhibits, the same catalytic triad of residues (Cys-His-Asp) in the active site.
About this Structure
2BSZ is a Single protein structure of sequence from Mesorhizobium loti. Active as Arylamine N-acetyltransferase, with EC number 2.3.1.5 Full crystallographic information is available from OCA.
Reference
Structure of Mesorhizobium loti arylamine N-acetyltransferase 1., Holton SJ, Dairou J, Sandy J, Rodrigues-Lima F, Dupret JM, Noble ME, Sim E, Acta Crystallograph Sect F Struct Biol Cryst Commun. 2005 Jan 1;61(Pt, 1):14-6. Epub 2004 Dec 24. PMID:16508079
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