5XHW

Crystal structure of HddC from Yersinia pseudotuberculosis

Summary for 5XHW

• Entry DOI: 10.2210/pdb5xhw/pdb
• Descriptor: Putative 6-deoxy-D-mannoheptose pathway protein, SULFATE ION (3 entities in total)
• Functional Keywords: nucleotransferase, hddc, transferase
• Biological source: Yersinia pseudotuberculosis
• Total number of polymer chains: 1
• Total formula weight: 27168.13

Authors

Park, J.,Kim, H.,Kim, S.,Shin, D.H. (deposition date: 2017-04-24, release date: 2018-04-25, Last modification date: 2024-11-13)

Primary citation

Kim, H.,Park, J.,Kim, S.,Shin, D.H.
Crystal structure of d-glycero-alpha-d-manno-heptose-1-phosphate guanylyltransferase from Yersinia pseudotuberculosis.
Biochim. Biophys. Acta, 1866:482-487, 2018

PubMed Abstract: The Gram-negative bacterium Yersinia pseudotuberculosis is the causative agent of yersiniosis. d-glycero-α-d-manno-heptose-1-phosphate guanylyltransferase (HddC) is the fourth enzyme of the GDP-d-glycero-α-d-manno-heptose 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 2.0Å 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.

PubMed: 29277661
DOI: 10.1016/j.bbapap.2017.12.005

Experimental method

X-RAY DIFFRACTION (2 Å)