Crystallization and preliminary X-ray crystallographic studies of VibE, a vibriobactin-specific 2,3-dihydroxybenzoate-AMP ligase from Vibrio cholerae

• Published in: Acta crystallographica. Section F, Structural biology and crystallization communications Vol. 67; no. 12; pp. 1563 - 1565
• Main Authors: Liu, Xiuhua, Wang, Zhi, Zhu, Deyu, Wei, Tiandi, Gu, Lichuan, Xu, Sujuan
• Format: Journal Article
• Language: English
• Published: 5 Abbey Square, Chester, Cheshire CH1 2HU, England International Union of Crystallography 01.12.2011
• Subjects: 2,3‐dihydroxybenzoate‐AMP ligase; 3-dihydroxybenzoate-AMP ligase; Asymmetry; Bacteriocins - metabolism; Crystallization; Crystallization Communications; Crystallography; Crystallography, X-Ray; Crystals; Lipase - chemistry; Lipase - metabolism; Proteins; Purification; Substrate Specificity; VibE; Vibrio; Vibrio cholerae; Vibrio cholerae - enzymology; vibriobactin biosynthesis; vibriobactin synthetases; X-rays
• ISSN: 1744-3091; 1744-3091
• DOI: 10.1107/S1744309111039005

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 P21, 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 Å3 Da−1 and solvent content of 24.41%.