3LNB

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

Summary for 3LNB

• Entry DOI: 10.2210/pdb3lnb/pdb
• Descriptor: N-acetyltransferase family protein, COENZYME A, FORMIC ACID, ... (4 entities in total)
• Functional Keywords: arylamine n-acetyltransferase, transferase, nat, acetyltransferase, acyltransferase
• Biological source: Bacillus anthracis
• Total number of polymer chains: 1
• Total formula weight: 36162.07

Authors

Li de la Sierra-Gallay, I.,Pluvinage, B.,Rodrigues-Lima, F. (deposition date: 2010-02-02, release date: 2011-01-26, Last modification date: 2023-11-01)

Primary citation

Pluvinage, B.,Li de la Sierra-Gallay, I.,Kubiak, X.,Xu, X.,Dairou, J.,Dupret, J.M.,Rodrigues-Lima, F.
The Bacillus anthracis arylamine N-acetyltransferase ((BACAN)NAT1) that inactivates sulfamethoxazole, reveals unusual structural features compared with the other NAT isoenzymes.
Febs Lett., 585:3947-3952, 2011

PubMed Abstract: 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.

PubMed: 22062153
DOI: 10.1016/j.febslet.2011.10.041

Experimental method

X-RAY DIFFRACTION (2.01 Å)