Literature DB >> 25005104

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

Ye Ji Jeon1, Wan Seok Song1, Sung-il Yoon1.   

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.

Entities:  

Keywords:  Bacillus subtilis; HD domain; YpgQ; phosphohydrolase

Mesh：

Substances：

Year:  2014        PMID： 25005104      PMCID： PMC4089547          DOI： 10.1107/S2053230X14006682

Source DB:  PubMed          Journal:  Acta Crystallogr F Struct Biol Commun        ISSN： 2053-230X            Impact factor:   1.056


  11 in total

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