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Crystal structure of D‐ glycero ‐ Β ‐D‐ manno ‐heptose‐1‐phosphate adenylyltransferase from Burkholderia pseudomallei
Author(s) -
Park Jimin,
Kim Hyojin,
Kim Suwon,
Lee Daeun,
Kim MiSun,
Shin Dong Hae
Publication year - 2018
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.25398
Subject(s) - heptose , stereochemistry , biosynthesis , chemistry , crystal structure , pyrophosphate , transferase , enzyme , active site , protein structure , biochemistry , crystallography , mutant , gene
The crystal structure of HldC from B. pseudomallei ( Bp HldC), the fourth enzyme of the heptose biosynthesis pathway, has been determined. Bp HldC 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 Bp HldC 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 Bp HldC indicate that the core catalytic mechanism of Bp HldC 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.