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Purification, crystallization and preliminary X-ray analysis of a putative nucleotide phosphohydrolase, YpgQ, from Bacillus subtilis.

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 P2? 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.

SUBMITTER: Jeon YJ

PROVIDER: S-EPMC4089547 | biostudies-literature | 2014 Jul

REPOSITORIES: biostudies-literature

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Purification, crystallization and preliminary X-ray analysis of a putative nucleotide phosphohydrolase, YpgQ, from Bacillus subtilis.

Jeon Ye Ji YJ Song Wan Seok WS Yoon Sung-il SI

Acta crystallographica. Section F, Structural biology communications 20140619 Pt 7

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 6 ...[more]

PMID: 25005104

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