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Structure paper

TitleMevalonate 5-diphosphate mediates ATP binding to the mevalonate diphosphate decarboxylase from the bacterial pathogen Enterococcus faecalis.
Journal, issue, pagesJ. Biol. Chem., Vol. 292, Page 21340-21351, Year 2017
Publish dateMar 5, 2017 (structure data deposition date)
AuthorsChen, C.L. / Mermoud, J.C. / Paul, L.N. / Steussy, C.N. / Stauffacher, C.V.
External linksJ. Biol. Chem. / PubMed:29025876
MethodsX-ray diffraction
Resolution1.989 - 2.1 Å
Structure data

PDB-5v2l:
Mevalonate diphosphate mediated ATP binding mechanism of the mevalonate diphosphate decarboxylase from Enterococcus faecalis
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

PDB-5v2m:
Mevalonate diphosphate mediated ATP binding mechanism of the mevalonate diphosphate decarboxylase from Enterococcus faecalis
Method: X-RAY DIFFRACTION / Resolution: 1.989 Å

Chemicals

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM

ChemComp-PO4:
PHOSPHATE ION

ChemComp-HOH:
WATER

ChemComp-SO4:
SULFATE ION

Source
  • enterococcus faecalis v583 (bacteria)
KeywordsLYASE / The mevalonate pathway / Vancomycin resistant enterococci / Enzyme kinetics / isothermal titration calorimetry.

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