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A preliminary X‐ray study of 3‐deoxy‐D‐ manno ‐oct‐2‐ulosonic acid 8‐phosphate phosphatase (YrbI) from Burkholderia pseudomallei
Author(s) -
Park Jimin,
Lee Daeun,
Kim MiSun,
Kim Dae Yong,
Shin Dong Hae
Publication year - 2015
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x15006135
Subject(s) - burkholderia pseudomallei , chemistry , phosphatase , phosphate , enzyme , acid phosphatase , biochemistry , biosynthesis , stereochemistry , bacteria , biology , genetics
3‐Deoxy‐D‐ manno ‐oct‐2‐ulosonic acid 8‐phosphate phosphatase (YrbI), the third enzyme in the pathway for the biosynthesis of 3‐deoxy‐D‐ manno ‐oct‐2‐ulosonic acid (KDO), hydrolyzes KDO 8‐phosphate to KDO and inorganic phosphate. YrbI belongs to the haloacid dehalogenase (HAD) superfamily, which is a large family of magnesium‐dependent phosphatase/phosphotransferase enzymes. In this study, YrbI from Burkholderia pseudomallei , the causative agent of melioidosis, has been cloned, expressed, purified and crystallized. Synchrotron X‐ray data were also collected to 2.25 Å resolution. The crystal belonged to the primitive orthorhombic space group P 2 1 2 1 2 1 , with unit‐cell parameters a = 63.7, b = 97.5, c = 98.0 Å. A full structural determination is in progress to elucidate the structure–function relationship of this protein.