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Structure paper

TitleMutation of archaeal isopentenyl phosphate kinase highlights mechanism and guides phosphorylation of additional isoprenoid monophosphates.
Journal, issue, pagesAcs Chem. Biol., Vol. 5, Page 589-601, Year 2010
Publish dateOct 5, 2009 (structure data deposition date)
AuthorsDellas, N. / Noel, J.P.
External linksAcs Chem. Biol. / PubMed:20392112
MethodsX-ray diffraction
Resolution2.05 - 2.7 Å
Structure data

PDB-3k4o:
Crystal Structure of Isopentenyl Phosphate Kinase from Methanocaldococcus jannaschii
Method: X-RAY DIFFRACTION / Resolution: 2.05 Å

PDB-3k4y:
Crystal Structure of Isopentenyl Phosphate Kinase from M. jannaschii in complex with IPP
Method: X-RAY DIFFRACTION / Resolution: 2.54 Å

PDB-3k52:
Crystal Structure of Isopentenyl Phosphate Kinase from M. jannaschii in complex with IP
Method: X-RAY DIFFRACTION / Resolution: 2.7 Å

PDB-3k56:
Crystal Structure of Isopentenyl Phosphate Kinase from M. jannaschii in complex with IPP beta-S
Method: X-RAY DIFFRACTION / Resolution: 2.34 Å

Chemicals

ChemComp-HG:
Unknown entry

ChemComp-SO4:
SULFATE ION

ChemComp-HOH:
WATER

ChemComp-IPE:
3-METHYLBUT-3-ENYL TRIHYDROGEN DIPHOSPHATE

ChemComp-IP8:
Isopentenyl phosphate

ChemComp-IS3:
Isopentenyl Diphosphate Beta-S

Source
  • methanocaldococcus jannaschii (archaea)
KeywordsTRANSFERASE / small molecule kinase / ATP-binding / Methanocaldococcus jannaschii / isopentenyl monophosphate / isopentenyl diphosphate / isoprenoid biosynthesis / mevalonate pathway / archaea / ATP gamma-S

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