Crystallization and preliminary X-ray analysis of XC1015, a histidine triad-like protein from Xanthomonas campestris.
Histidine-triad (HIT) proteins are a superfamily of nucleotide hydrolases and transferases that contain a conserved Hphi Hphi Hphi phi motif (where phi is a hydrophobic amino acid) and are found in a variety of organisms. In addition to binding to a variety of nucleotides, other biological functions of the HIT superfamily proteins have been discovered and HIT malfunction has been implicated in several human diseases. Structural studies of HIT superfamily proteins are thus of particular interest. In this manuscript, the cloning, expression, crystallization and preliminary X-ray analysis of XC1015, a HIT protein present in the plant pathogen Xanthomonas campestris pathovar campestris, are reported. The XC1015 crystals diffracted to a resolution of 1.3 A. They are tetragonal and belong to space group P4(3)2(1)2, with unit-cell parameters a = 40.52, b = 40.52, c = 126.89 A.
Lo
Wen-Ting
WT
Institute of Biochemistry, National Chung-Hsing University, Taichung 40227, Taiwan.
Chin
Ko-Hsin
KH
Shr
Hui-Lin
HL
Gao
Fei Philip
FP
Lyu
Ping-Chiang
PC
Wang
Andrew H-J
AH
Chou
Shan-Ho
SH
D001426:Bacterial Proteins / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray; D006867:Hydrolases / Q000737:chemistry*; D016959:Xanthomonas campestris / Q000737:chemistry*
D001426:Bacterial Proteins; C097552:histidine triad protein; D006867:Hydrolases