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Crystal structure of D-glycero-B-D-manno-heptose-1-phosphate adenylyltransferase from Burkholderia pseudomallei
- Crystal structure of D-glycero-B-D-manno-heptose-1-phosphate adenylyltransferase from Burkholderia pseudomallei
- Park, Jimin; Kim, Hyojin; Kim, Suwon; Lee, Daeun; Kim, Mi-Sun; Shin, Dong Hae
- Ewha Authors
- 신동해; 김수원; 김미선
- SCOPUS Author ID
- 신동해; 김수원
- Issue Date
- Journal Title
- PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS
- PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS vol. 86, no. 1, pp. 124 - 131
- heptose biosynthesis pathway; HldC; lipopolysaccharide; melioidosis; nucleotidyltransferase
- SCI; SCIE; SCOPUS
- Document Type
- 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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