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Structure paper

TitleCrystal Structures of Mutant IspH Proteins Reveal a Rotation of the Substrate's Hydroxymethyl Group during Catalysis.
Journal, issue, pagesJ. Mol. Biol., Vol. 416, Page 1-9, Year 2012
Publish dateJul 19, 2011 (structure data deposition date)
AuthorsSpan, I. / Grawert, T. / Bacher, A. / Eisenreich, W. / Groll, M.
External linksJ. Mol. Biol. / PubMed:22137895
MethodsX-ray diffraction
Resolution1.4 - 2.1 Å
Structure data

PDB-3szl:
IspH:Ligand Mutants - wt 70sec
Method: X-RAY DIFFRACTION / Resolution: 1.6 Å

PDB-3szo:
IspH:HMBPP complex after 3 minutes X-ray pre-exposure
Method: X-RAY DIFFRACTION / Resolution: 1.6 Å

PDB-3szu:
IspH:HMBPP complex structure of E126Q mutant
Method: X-RAY DIFFRACTION / Resolution: 1.4 Å

PDB-3t0f:
IspH:HMBPP (substrate) structure of the E126D mutant
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

PDB-3t0g:
IspH:HMBPP (substrate) structure of the T167C mutant
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

Chemicals

ChemComp-SF4:
IRON/SULFUR CLUSTER

ChemComp-H6P:
(2E)-4-hydroxy-3-methylbut-2-en-1-yl trihydrogen diphosphate

ChemComp-HOH:
WATER

ChemComp-F3S:
FE3-S4 CLUSTER

Source
  • escherichia coli (E. coli)
KeywordsOXIDOREDUCTASE / 4Fe-4S iron-sulfur cluster / conserved cysteine / induced fit mechanism / IPP and DMAPP production final step / non-mevalonate pathway / substrate HMBPP / alternate conformations / 3Fe-4S iron-sulfur cluster / low activity

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