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TitleStructural Analysis of Thermus Thermophilus Hb27 Mannosyl-3-Phosphoglycerate Synthase Provides Evidence for a Second Catalytic Metal Ion and New Insight Into the Retaining Mechanism of Glycosyltransferases.
Journal, issue, pagesJ. Biol. Chem., Vol. 285, Page 17857-, Year 2010
Publish dateOct 19, 2009 (structure data deposition date)
AuthorsGoncalves, S. / Borges, N. / Esteves, A.M. / Victor, B. / Soares, C.M. / Santos, H. / Matias, P.M.
External linksJ. Biol. Chem. / PubMed:20356840
MethodsX-ray diffraction
Resolution2.806 - 2.977 Å
Structure data

PDB-2wvk:
Mannosyl-3-phosphoglycerate synthase from Thermus thermophilus HB27 apoprotein
Method: X-RAY DIFFRACTION / Resolution: 2.97 Å

PDB-2wvl:
Mannosyl-3-phosphoglycerate synthase from Thermus thermophilus HB27 in complex with GDP-alpha-D-Mannose and Mg(II)
Method: X-RAY DIFFRACTION / Resolution: 2.806 Å

PDB-2wvm:
H309A mutant of Mannosyl-3-phosphoglycerate synthase from Thermus thermophilus HB27 in complex with GDP-alpha-D-Mannose and Mg(II)
Method: X-RAY DIFFRACTION / Resolution: 2.977 Å

Chemicals

ChemComp-FLC:
CITRATE ANION

ChemComp-ZN:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-GDD:
GUANOSINE-5'-DIPHOSPHATE-ALPHA-D-MANNOSE

ChemComp-MG:
Unknown entry

Source
  • thermus thermophilus (bacteria)
KeywordsTRANSFERASE / GT-A FOLD / GLYCOSYLTRANSFERASE / RETAINING MECHANISM / GLUCOSYL TRANSFERASE

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