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

Title
Crystal structure of D-glycero-B-D-manno-heptose-1-phosphate adenylyltransferase from Burkholderia pseudomallei
Authors
Park, JiminKim, HyojinKim, SuwonLee, DaeunKim, Mi-SunShin, Dong Hae
Ewha Authors
신동해김수원김미선
SCOPUS Author ID
신동해scopus; 김수원scopus
Issue Date
2018
Journal Title
PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS
ISSN
0887-3585JCR Link

1097-0134JCR Link
Citation
PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS vol. 86, no. 1, pp. 124 - 131
Keywords
heptose biosynthesis pathwayHldClipopolysaccharidemelioidosisnucleotidyltransferase
Publisher
WILEY
Indexed
SCI; SCIE; SCOPUS WOS scopus
Document Type
Article
Abstract
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.
DOI
10.1002/prot.25398
Appears in Collections:
약학대학 > 약학과 > Journal papers
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