A preliminary X-ray study of 3-deoxy-d-manno-oct-2-ulosonic acid 8-phosphate phosphatase (YrbI) from Burkholderia pseudomallei

Jimin Park, Daeun Lee, Mi Sun Kim, Dae Yong Kim, Dong Hae Shin

Research output: Contribution to journalArticlepeer-review

2 Scopus citations

Abstract

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/phospho transferase 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 P212121, 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.

Original languageEnglish
Pages (from-to)790-793
Number of pages4
JournalActa Crystallographica Section F:Structural Biology Communications
Volume71
DOIs
StatePublished - 1 Jun 2015

Bibliographical note

Publisher Copyright:
© 2015 International Union of Crystallography.

Keywords

  • 3-deoxy-d-manno-oct-2-ulosonic acid 8-phosphate phosphatase
  • Burkholderia pseudomallei
  • YrbI

Fingerprint

Dive into the research topics of 'A preliminary X-ray study of 3-deoxy-d-manno-oct-2-ulosonic acid 8-phosphate phosphatase (YrbI) from Burkholderia pseudomallei'. Together they form a unique fingerprint.

Cite this