Crystal structure of D-glycero-B-D-manno-heptose-1-phosphate adenylyltransferase from Burkholderia pseudomallei
- 주제(키워드) heptose biosynthesis pathway , HldC , lipopolysaccharide , melioidosis , nucleotidyltransferase
- 주제(기타) Biochemistry & Molecular Biology; Biophysics
- 설명문(일반) [Park, Jimin; Kim, Hyojin; Kim, Suwon; Lee, Daeun; Kim, Mi-Sun; Shin, Dong Hae] Ewha W Univ, Coll Pharm, Seoul, South Korea
- 등재 SCIE, SCOPUS
- 발행기관 WILEY
- 발행년도 2018
- URI http://www.dcollection.net/handler/ewha/000000150085
- 본문언어 영어
- Published As http://dx.doi.org/10.1002/prot.25398
초록/요약
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--d-manno-heptose-1-phosphate into ADP-d-glycero--d-manno-heptose and pyrophosphate. The crystal structure of BpHldC belongs to the nucleotidyltransferase / phosphodiesterase superfamily sharing a common Rossmann-like / 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.
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