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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 Link1097-0134JCR Link
Citation
vol. 86, no. 1, pp. 124 - 131
Keywords
heptose biosynthesis pathwayHldClipopolysaccharidemelioidosisnucleotidyltransferase
Publisher
WILEY
Indexed
SCI; SCIE; SCOPUS WOS scopus
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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