› 1jcs

X-ray diffraction
2.2Å resolution

CRYSTAL STRUCTURE OF RAT PROTEIN FARNESYLTRANSFERASE COMPLEXED WITH THE PEPTIDE SUBSTRATE TKCVFM AND AN ANALOG OF FARNESYL DIPHOSPHATE

Released:
DOI: 10.2210/pdb1jcs/pdb
PDB entry 1jcs coloured by chain, front view.
PDB entry 1jcs coloured by chain, side view.
PDB entry 1jcs coloured by chain, top view.
Source organism: Rattus norvegicus
Primary publication:
The crystal structure of human protein farnesyltransferase reveals the basis for inhibition by CaaX tetrapeptides and their mimetics.
Long SB, Hancock PJ, Kral AM, Hellinga HW, Beese LS
Proc Natl Acad Sci U S A 98 12948-53 (2001)
PMID: 11687658

Function and Biology Details

Reactions catalysed: 
Farnesyl diphosphate + protein-cysteine = S-farnesyl protein + diphosphate
Geranylgeranyl diphosphate + protein-cysteine = S-geranylgeranyl-protein + diphosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-162258 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha Chain: A
Molecule details ›
Chain: A
Length: 377 amino acids
Theoretical weight: 44.1 KDa
Source organism: Rattus norvegicus
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: Q04631 (Residues: 1-377; Coverage: 100%)
Gene name: Fnta
Sequence domains: Protein prenyltransferase alpha subunit repeat
Structure domains: Protein prenylyltransferase
Protein farnesyltransferase subunit beta Chain: B
Molecule details ›
Chain: B
Length: 437 amino acids
Theoretical weight: 48.72 KDa
Source organism: Rattus norvegicus
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: Q02293 (Residues: 1-437; Coverage: 100%)
Gene name: Fntb
Sequence domains: Prenyltransferase and squalene oxidase repeat
Structure domains: Glycosyltransferase
SYNTHETIC HEXAPEPTIDE TKCVFM Chain: C
Molecule details ›
Chain: C
Length: 6 amino acids
Theoretical weight: 729 Da

Ligands and Environments

3 bound ligands:
Ligand ZN 1 x ZN
Ligand FII 1 x FII
Ligand ACY 2 x ACY
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P61
Unit cell:
a: 170.921Å b: 170.921Å c: 69.425Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.162 0.16 0.202
Expression system: Spodoptera frugiperda

Quick links

Citations

10 review citations

Lipid posttranslational modifications. Farnesyl transferase inhibitors.
Basso et al. (2006)
9 more

1 mention without citation

The crystal structure of human protein farnesyltransferase reveals the basis for inhibition by CaaX tetrapeptides and their mimetics.
Long et al. (2001)