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Expression and crystallographic studies of d ‐ glycero ‐β‐ d ‐ manno ‐heptose‐1‐phosphate adenylyltransferase from Burkholderia pseudomallei
Author(s) -
Park Jimin,
Kim Hyojin,
Kim Suwon,
Lee Daeun,
Shin Dong Hae
Publication year - 2017
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/s2053230x16020537
Subject(s) - burkholderia pseudomallei , burkholderia , chemistry , stereochemistry , bacteria , microbiology and biotechnology , biology , genetics
The Gram‐negative bacterium Burkholderia pseudomallei is the causative agent of melioidosis. d ‐ glycero ‐β‐ d ‐ manno ‐Heptose‐1‐phosphate adenylyltransferase (HldC) is the fourth enzyme of the ADP‐ l ‐ glycero ‐β‐ d ‐ manno ‐heptose biosynthesis pathway, which produces an essential carbohydrate comprising the inner core of lipopolysaccharide. Therefore, HldC is a potential target of antibiotics against melioidosis. In this study, HldC from B. pseudomallei has been cloned, expressed, purified and crystallized. Synchrotron X‐ray data from a selenomethionine‐substituted HldC crystal were also collected to 2.8 Å resolution. The crystal belonged to the primitive triclinic space group P 1, with unit‐cell parameters a = 74.0, b = 74.0, c = 74.9 Å, α = 108.4, β = 108.4, γ = 108.0°. Eight protomers are present in the unit cell and three out of five selenomethionines were found in each protomer using the PHENIX software suite. A full structural determination is in progress to elucidate the structure–function relationship of the protein.