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Structure paper

TitleStructure and mechanism of an Arabidopsis medium/long-chain-length prenyl pyrophosphate synthase
Journal, issue, pagesPlant Physiol., Vol. 155, Page 1079-1090, Year 2011
Publish dateOct 24, 2010 (structure data deposition date)
AuthorsHsieh, F.-L. / Chang, T.-H. / Ko, T.-P. / Wang, A.H.-J.
External linksPlant Physiol. / PubMed:21220764
MethodsX-ray diffraction
Resolution2.6 - 2.65 Å
Structure data

PDB-3apz:
Apo form of Arabidopsis medium/long-chain length prenyl pyrophosphate synthase
Method: X-RAY DIFFRACTION / Resolution: 2.6 Å

PDB-3aq0:
Ligand-bound form of Arabidopsis medium/long-chain length prenyl pyrophosphate synthase (surface polar residue mutant)
Method: X-RAY DIFFRACTION / Resolution: 2.65 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-MG:
Unknown entry

ChemComp-FPP:
FARNESYL DIPHOSPHATE

ChemComp-ISY:
3-methylbut-3-enylsulfanyl(phosphonooxy)phosphinic acid

ChemComp-PPV:
PYROPHOSPHATE

ChemComp-PEG:
DI(HYDROXYETHYL)ETHER

Source
  • arabidopsis thaliana (thale cress)
KeywordsTRANSFERASE / prenyltransferase / All alpha-helices fold / chroloplast / isoprenoid biosynthetic process

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