PDBsum entry: 2bsz

Transferase

PDB id: 2bsz

Contents

Protein chains

267 a.a. *

Waters ×256

* Residue conservation analysis

PDB id:

2bsz

Name:

Transferase

Title:

Structure of mesorhizobium loti arylamine n- acetyltransferase 1

Structure:

Arylamine n-acetyltransferase 1. Chain: a, b. Engineered: yes

Source:

Rhizobium loti. Organism_taxid: 381. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

2.00Å R-factor: 0.198 R-free: 0.249

Authors:

S.J.Holton,J.Dairou,J.Sandy,F.Rodrigues-Lima,J.-M.Dupret, M.E.M.Noble,E.Sim

Key ref:

S.J.Holton et al. (2005). Structure of Mesorhizobium loti arylamine N-acetyltransferase 1. Acta Crystallograph Sect F Struct Biol Cryst Commun, 61, 14-16. PubMed id: 16508079 DOI: 10.1107/S1744309104030659

Date:

24-May-05 Release date: 25-May-05

Protein chains

Q98D42  (Q98D42_RHILO) -  Arylamine N-acetyltransferase

Seq: 278 a.a.

Struc: 267 a.a.

Enzyme reactions

• Enzyme class: E.C.2.3.1.5 - Arylamine N-acetyltransferase.
• Reaction: Acetyl-CoA + an arylamine = CoA + an N-acetylarylamine

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 Gene Ontology (GO) functional annotation 

• Biological process: metabolic process (1 term)
• Biochemical function: transferase activity (4 terms)

reference

DOI no: 10.1107/S1744309104030659

Acta Crystallograph Sect F Struct Biol Cryst Commun 61:14-16 (2005)

PubMed id: 16508079

Structure of Mesorhizobium loti arylamine N-acetyltransferase 1.

S.J.Holton, J.Dairou, J.Sandy, F.Rodrigues-Lima, J.M.Dupret, M.E.Noble, E.Sim.

ABSTRACT

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.

Selected figure(s)

Figure 1.
Figure 1 X-ray crystal structure of M. loti NAT1. (a) and (b) Orthogonal secondary-structure representation of M. loti NAT1 (mauve) superimposed with worm representations of the NAT structures from Salmonella typhimurium (cyan; PDB code 1e2t ), Mycobacterium smegmatis (yellow; PDB code 1gx3 ) and Pseudomonas aeruginosa (green; PDB code 1w4t ) using the program O (Jones et al., 1991[Jones, T. A., Zou, J. Y., Cowan, S. W. & Kjeldgaard, M. (1991). Acta Cryst. A47, 110-119.]). The M. loti NAT1 active-site catalytic triad is also shown in ball-and-stick representation. (c) Surface representation of M. smegmatis NAT1 (yellow) and M. loti NAT1 (mauve) in the region of the active-site entrance. Underlying secondary-structural elements are drawn in a similar colour scheme. For clarity, the 6 helix, corresponding to residues 183-205 in the M. loti structure, is not shown in this figure. The active-site catalytic triad is also shown in ball-and-stick mode to aid orientation. All images were generated using AESOP (M. E. M. Noble, Oxford University, England).

The above figure is reprinted from an Open Access publication published by the IUCr: Acta Crystallograph Sect F Struct Biol Cryst Commun (2005, 61, 14-16) copyright 2005.