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Structure paper

TitleConversion of protein farnesyltransferase to a geranylgeranyltransferase.
Journal, issue, pagesBiochemistry, Vol. 45, Page 9746-9755, Year 2006
Publish dateMay 31, 2006 (structure data deposition date)
AuthorsTerry, K.L. / Casey, P.J. / Beese, L.S.
External linksBiochemistry / PubMed:16893176
MethodsX-ray diffraction
Resolution1.5 - 3 Å
Structure data

PDB-2h6f:
Protein Farnesyltransferase Complexed with a Farnesylated DDPTASACVLS Peptide Product at 1.5A Resolution
Method: X-RAY DIFFRACTION / Resolution: 1.5 Å

PDB-2h6g:
W102T Protein Farnesyltransferase Mutant Complexed with a Geranylgeranylated DDPTASACVLS Peptide Product at 1.85A Resolution
Method: X-RAY DIFFRACTION / Resolution: 1.85 Å

PDB-2h6h:
Y365F Protein Farnesyltransferase Mutant Complexed with a Farnesylated DDPTASACVLS Peptide Product at 1.8A
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

PDB-2h6i:
W102T/Y365F Protein Farnesyltransferase Double Mutant Complexed with a Geranylgeranylated DDPTASACVLS Peptide Product at 3.0A
Method: X-RAY DIFFRACTION / Resolution: 3 Å

Chemicals

ChemComp-ACY:
ACETIC ACID

ChemComp-ZN:
Unknown entry

ChemComp-FAR:
FARNESYL

ChemComp-HOH:
WATER

ChemComp-GER:
GERAN-8-YL GERAN

Source
  • homo sapiens (human)
KeywordsTRANSFERASE / FTase / farnesyltransferase / farnesyl transferase / prenyltransferase / CaaX / Ras / lipid modification / prenylation / substrate selectivity

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