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Crystal structure of D-glycero-alpha-D-manno-heptose-1-phosphate guanylyltransferase from Yersinia pseudotuberculosis

Title
Crystal structure of D-glycero-alpha-D-manno-heptose-1-phosphate guanylyltransferase from Yersinia pseudotuberculosis
Authors
Kim, HyojinPark, JiminKim, SuwonShin, Dong Hae
Ewha Authors
신동해김수원
SCOPUS Author ID
신동해scopus; 김수원scopus
Issue Date
2018
Journal Title
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS
ISSN
1570-9639JCR Link

0006-3002JCR Link
Citation
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS vol. 1866, no. 3, pp. 482 - 487
Keywords
Glycosyltransferase a type superfamilylD-glycero-alpha-D-manno-heptose-1-phosphate guanylyltransferase (HddC)GDP-D-glycero-alpha-D-manno-heptose biosynthesis pathwayYersiniosisX-ray crystal structure
Publisher
ELSEVIER SCIENCE BV
Indexed
SCI; SCIE; SCOPUS WOS scopus
Document Type
Article
Abstract
The Gram-negative bacterium Yersinia pseudotuberculosis is the causative agent of yersiniosis. D-glycero-alpha-D-manno-heptose-1-phosphate guanylyltransferase (HddC) is the fourth enzyme of the GDP-D-glycero-alpha-D-mannoheptose biosynthesis pathway which is important for the virulence of the microorganism. Therefore, HddC is a potential target of antibiotics against yersiniosis. In this study, HddC from the synthesized HddC gene of Y. pseudotuberculosis has been expressed, purified, crystallized. Synchrotron X-ray data from a selenomethionine-substituted HddC crystal were also collected and its structure was determined at 2.0 angstrom resolution. Structure analyses revealed that it belongs to the glycosyltransferase A type superfamily members with the signature motif GXGXR for nucleotide binding. Despite of remarkable structural similarity, HddC uses GTP for catalysis instead of CTP and UTP which are used for other major family members, cytidylyltransferase and uridylyltransferase, respectively. We suggest that EXXPLGTGGA and L(S/A/G)X(S/G) motifs are probably essential to bind with GTP and a FSFE motif with substrate.
DOI
10.1016/j.bbapap.2017.12.005
Appears in Collections:
약학대학 > 약학과 > Journal papers
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