Crystal structure of D-glycero-Β-D-manno-heptose-1-phosphate adenylyltransferase from Burkholderia pseudomallei

Jimin Park, Hyojin Kim, Suwon Kim, Daeun Lee, Mi Sun Kim, Dong Hae Shin

Research output: Contribution to journalArticlepeer-review

6 Scopus citations


The crystal structure of HldC from B. pseudomallei (BpHldC), the fourth enzyme of the heptose biosynthesis pathway, has been determined. BpHldC converts ATP and d-glycero-β-d-manno-heptose-1-phosphate into ADP-d-glycero-β-d-manno-heptose and pyrophosphate. The crystal structure of BpHldC belongs to the nucleotidyltransferase α/β phosphodiesterase superfamily sharing a common Rossmann-like α/β fold with a conserved T/HXGH sequence motif. The invariant catalytic key residues of BpHldC indicate that the core catalytic mechanism of BpHldC may be similar to that of other closest homologues. Intriguingly, a reorientation of the C-terminal helix seems to guide open and close states of the active site for the catalytic reaction.

Original languageEnglish
Pages (from-to)124-131
Number of pages8
JournalProteins: Structure, Function and Bioinformatics
Issue number1
StatePublished - Jan 2018


  • HldC
  • heptose biosynthesis pathway
  • lipopolysaccharide
  • melioidosis
  • nucleotidyltransferase


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