Crystallization and preliminary crystallographic analysis of a D-aminoacylase from Alcaligenes faecalis DA1.
D-Aminoacylases catalyze the hydrolysis of N-acyl-D-amino acids into D-amino acids with the aid of zinc ions. The first D-aminoacylase crystal from Alcaligenes faecalis has been obtained in hanging drops at pH 5.6 by the vapour-diffusion method using 30% polyethylene glycol 4000 as precipitant. It belongs to space group P2(1)2(1)2(1), with unit-cell parameters a = 60.2, b = 76.6, c = 135.3 A. Reflections to 1.2 A resolution are observable. An initial atomic model with 472 residues has been built based on SeMet SAD data at 1.8 A resolution. Unexpectedly, the structure revealed a novel metal centre in the amidohydrolase superfamily.
Institute of Biochemistry, National Yang-Ming University, Taipei, Taiwan.
Cheng Sheng
CS
Hsu
Shen Jia
SJ
Chen
Ying Chieh
YC
Tsai
Ting Wan
TW
Lin
Shwu Huey
SH
Liaw
Andrew H J
AH
Wang
D000421:Alcaligenes / Q000201:enzymology*; D000581:Amidohydrolases / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray; D015394:Molecular Structure; D011487:Protein Conformation
D000581:Amidohydrolases; C019672:aminoacylase I