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Literature summary extracted from

  • Kim, H.; Park, J.; Kim, S.; Shin, D.H.
    Crystal structure of D-glycero-alpha-D-manno-heptose-1-phosphate guanylyltransferase from Yersinia pseudotuberculosis (2018), Biochim. Biophys. Acta, 1866, 482-487 .
    View publication on PubMed

Application

EC Number Application Comment Organism
2.7.7.71 drug development HddC is a potential target of antibiotics against yersiniosis Yersinia pseudotuberculosis

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.7.71 gene YphddC, recombinant expression of His6-tagged wild-type enzyme in Escherichia coli strain BL21(DE3), recombinant expression of SeMet-labeled enzyme in Escherichia coli strain B834(DE3) Yersinia pseudotuberculosis

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.7.7.71 purified recombinant His6-tagged wild-type and SeMet-labeled enzymes with bound GMPPNP and Mg2+, hanging drop vapor diffusion method, mixing of 800 nl of 12 mg/ml protein in 20 mM HEPES, pH 7.5, with 800 nl of reservoir solution containing 0.1 M HEPES, pH 7.4, and 1.8 M ammonium sulfate for the wild-type, and 0.1 M HEPES, pH 7.0, and 2.2 M ammonium sulfate for the labeled enzyme, equilibration against 0.20 ml reservoir solution, method optimization, X-ray diffraction structure determination and analysis at 1.9-2.0 A resolution, modeling Yersinia pseudotuberculosis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.7.71 D-glycero-alpha-D-manno-heptose 1-phosphate + GTP Yersinia pseudotuberculosis
-
 GDP-D-glycero-alpha-D-manno-heptose + diphosphate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.7.7.71 Yersinia pseudotuberculosis Q8GJ90 serotype I
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.7.71 recombinant His6-tagged wild-type and SeMet-labeled enzymes from Escherichia coli by nickel affinity chromatography Yersinia pseudotuberculosis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.7.71 D-glycero-alpha-D-manno-heptose 1-phosphate + GTP
-
 Yersinia pseudotuberculosis GDP-D-glycero-alpha-D-manno-heptose + diphosphate
-
 ?

Subunits

EC Number Subunits Comment Organism
2.7.7.71 monomer crystal structure analysis Yersinia pseudotuberculosis
2.7.7.71 More structure comparisons, overview Yersinia pseudotuberculosis

Synonyms

EC Number Synonyms Comment Organism
2.7.7.71 D-glycero-alpha-D-manno-heptose-1-phosphate guanylyltransferase
-
 Yersinia pseudotuberculosis
2.7.7.71 HddC
-
 Yersinia pseudotuberculosis
2.7.7.71 YphddC
-
 Yersinia pseudotuberculosis

General Information

EC Number General Information Comment Organism
2.7.7.71 evolution structure analyses reveals that enzyme HddC 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. The EXXPLGTGGA and L(S/A/G)X(S/G) motifs are probably essential to bind with GTP and a FSFE motif with substrate Yersinia pseudotuberculosis
2.7.7.71 metabolism the enzyme HddC is part of the GDP-D-glycero-alpha-D-manno-heptose biosynthesis pathway, overview Yersinia pseudotuberculosis
2.7.7.71 additional information EXXPLGTGGA and L(S/A/G)X(S/G) motifs are probably essential to bind with GTP and a FSFE motif with substrate. The GXGXR (10GLGTR14 in YpHddC) sequence is the nucleotidyltransferase signature motif participating in interaction with the diphosphate moiety of GTP through their backbone nitrogens. The positively charged surface of this motif is significantly enhanced by the side chain of Arg14 and thus compensates the negative charge of the diphosphate. The side chain of Lys24 also seems to take part in the interaction with the diphosphate Yersinia pseudotuberculosis