来自枯草芽孢杆菌的一种假定核苷酸磷酸水解酶YpgQ的纯化、结晶及初步X射线分析。
Purification, crystallization and preliminary X-ray analysis of a putative nucleotide phosphohydrolase, YpgQ, from Bacillus subtilis.
作者信息
Jeon Ye Ji, Song Wan Seok, Yoon Sung-il
机构信息
Department of Systems Immunology, College of Biomedical Science, Kangwon National University, Chuncheon 200-701, Republic of Korea.
出版信息
Acta Crystallogr F Struct Biol Commun. 2014 Jul;70(Pt 7):984-6. doi: 10.1107/S2053230X14006682. Epub 2014 Jun 19.
Abstract
The histidine-aspartate (HD) domain exerts phosphohydrolase activity on nucleotides and functions in nucleotide metabolism. Sequence analysis suggested that YpgQ from Bacillus subtilis contains the HD domain, but the structure and function of YpgQ remain to be revealed. The recombinant YpgQ protein was overexpressed in an Escherichia coli cell expression system and was purified to homogeneity by Ni-NTA affinity and anion-exchange chromatography. Crystals in space group P2₁ were obtained in PEG 600 solutions and diffracted X-rays to 2.3 Å resolution. Moreover, X-ray fluorescence scans on YpgQ crystals demonstrated the metal-binding ability of YpgQ.
摘要
组氨酸-天冬氨酸（HD）结构域对核苷酸发挥磷酸水解酶活性，并在核苷酸代谢中起作用。序列分析表明，来自枯草芽孢杆菌的YpgQ含有HD结构域，但YpgQ的结构和功能仍有待揭示。重组YpgQ蛋白在大肠杆菌细胞表达系统中过表达，并通过镍-氮三乙酸亲和层析和阴离子交换层析纯化至同质。在聚乙二醇600溶液中获得了空间群为P2₁的晶体，其X射线衍射分辨率达到2.3 Å。此外，对YpgQ晶体的X射线荧光扫描证明了YpgQ的金属结合能力。
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