› 1o1t

X-ray diffraction
2.1Å resolution

Structure of FPT bound to the CVIM-FPP product

Released:
DOI: 10.2210/pdb1o1t/pdb
PDB entry 1o1t coloured by chain, front view.
PDB entry 1o1t coloured by chain, side view.
PDB entry 1o1t coloured by chain, top view.
Source organism: Rattus norvegicus
Primary publication:
Biochemical and structural studies with prenyl diphosphate analogues provide insights into isoprenoid recognition by protein farnesyl transferase.
Turek-Etienne TC, Strickland CL, Distefano MD
Biochemistry 42 3716-24 (2003)
PMID: 12667062

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 dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-554235 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha Chain: A
Molecule details ›
Chain: A
Length: 380 amino acids
Theoretical weight: 44.37 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli
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: 427 amino acids
Theoretical weight: 47.75 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q02293 (Residues: 1-427; Coverage: 98%)
Gene name: Fntb
Sequence domains: Prenyltransferase and squalene oxidase repeat
Structure domains: Glycosyltransferase

Ligands and Environments

3 bound ligands:
Ligand MG 1 x MG
Ligand ZN 1 x ZN
Ligand 2NH 1 x 2NH
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P61
Unit cell:
a: 171.44Å b: 171.44Å c: 69.22Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.198 0.198 not available
Expression system: Escherichia coli

Quick links

Citations

7 review citations

Thematic review series: lipid posttranslational modifications. Structural biology of protein farnesyltransferase and geranylgeranyltransferase type I.
Lane et al. (2006)
6 more