Open AccessCrystallization and preliminary X‐ray crystallographic studies of VibE, a vibriobactin‐specific 2,3‐dihydroxybenzoate‐AMP ligase from Vibrio cholerae
Author(s) -
Liu Xiuhua,
Wang Zhi,
Zhu Deyu,
Wei Tiandi,
Gu Lichuan,
Xu Sujuan
Publication year - 2011
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309111039005
Subject(s) - vibrio cholerae , crystallization , dna ligase , crystallography , crystal structure , escherichia coli , chemistry , crystal (programming language) , biology , stereochemistry , bacteria , enzyme , biochemistry , gene , genetics , organic chemistry , computer science , programming language
Vibriobactin synthetases (VibABCDEFH) catalyze the biosynthesis of vibriobactin in the pathogenic bacterium Vibrio cholerae . VibE, a vibriobactin‐specific 2,3‐dihydroxybenzoate‐AMP ligase, plays a critical role in the transfer of 2,3‐dihydroxybenzoate to the aryl carrier protein domain of holo VibB. Here, the cloning, protein expression and purification, crystallization and preliminary X‐ray crystallographic analysis of VibE from V. cholerae are reported. The VibE crystal diffracted to 2.3 Å resolution. The crystal belonged to space group P 2 1 , with unit‐cell parameters a = 56.471, b = 45.927, c = 77.014 Å, β = 95.895°. There is one protein molecule in the asymmetric unit, with a corresponding Matthews coefficient of 1.63 Å 3 Da −1 and solvent content of 24.41%.