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2.5.1.58: protein farnesyltransferase

This is an abbreviated version!
For detailed information about protein farnesyltransferase, go to the full flat file.

Word Map on EC 2.5.1.58

Reaction

farnesyl diphosphate
+
protein-cysteine
=
S-farnesyl protein
 +
diphosphate

Synonyms

AfFTase, CAAX farnesyltransferase, EhFT, Era1, farnesyl protein transferase, farnesyltransferase, farnesyltransferase ternary complex part II, farnesyltransferase, farnesyl pyrophosphate-protein, farnesyltransferase, protein, FntA, FntB, FPT, fptase, FTase, hFTase, HIT5, Pf-PFT, PfPFT, PFT, PFTase, prenyl transferase, prenylprotein transferase, prenyltransferase, protein cysteine farnesyltransferase, protein farnesyl transferase, protein farnesyltransferase, protein prenyltransferase, protein-farnesyltransferase, R-PFT, Ram1, RAS farnesyltransferase, Ras protein farnesyltransferase, rFPTase, rFTase, rPFTase, TbFTase, yPFTase

ECTree

     2 Transferases
         2.5 Transferring alkyl or aryl groups, other than methyl groups
             2.5.1 Transferring alkyl or aryl groups, other than methyl groups (only sub-subclass identified to date)
                2.5.1.58 protein farnesyltransferase

Crystallization

Crystallization on EC 2.5.1.58 - protein farnesyltransferase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified enzyme in complex with substrate farnesyl diphosphate, and inhibitors FPT-II-KCVVM, tipifarnib, andin ternary complex with farnesyl diphosphate and inhibitor ED5, X-ray diffraction structure determination and analysis at 1.45-1.90 A resolution, structure modelling
-
analysis of reaction mechanism using catalytically active crystals and comparison with the human enzyme. In the CAAX binding site, a single residue substitution at the a2 site from tyrosine to asparagine results in a deeper cavity in this region compared with the human enzyme. The prenylated product exit groove is wider in the Cryptococcus neoformans enzyme relative to human enzyme and varies in amino acid composition. A substrate-induced conformational change observed for the 4alpha-5alpha loop of results in a molecular surface in the active site with two distinct states that can be individually exploited for inhibitor design
-
crystal structure of FTase complexed with FPP and L-778,123
-
FTase in ternary complexes with an FPP analog and peptides derived from the cognate substrates H-Ras (GCVLS) and Rap2a (DDPTA-SACNIQ), the cross-reactive substrate TC21 (KKSKTKCVIF), and the non-substrate Rap2b (TKCVIL). Structures of GGTase-I in ternary complexes with a GGPP analog (3'azaGGPP) and peptides derived from the cognate substrates Cdc42 splice isoform 2 (RRCVLL Ca1a2X motif) and the heterotrimeric G protein g2 subunit (FREKKFFCAIL), and the cross-reactive substrates RhoB (GCINCCKVL), K-Ras4B (KKKSKTKCVIM) and TC21
-
molecular docking of inhibitors
a new crystalline form of enzyme for the mutant truncated 10 residues at the C-terminus
-
at 2.25 Angstrom, zinc occurs at a junction between a hydrophilic surface groove near the subunit interface: peptide binding site, and a deep lipophilic cleft in the beta subunit lined with aromatic residues: farnesyl diphosphate binding site
-
farnesyl diphosphate and peptide substrate can be accommodated in the hydrophobic active-site barrel, with the sole charged residue inside the barrel, Arg202 of the beta-subunit, forming a salt bridge with the negatively charged carboxy terminus of peptide substrate
-
molecular dynamics simulations to study enzyme flexibility in the 4 key intermediate states formed during the FTase catalytic mechanisms, ie. FTase resting state, binary complex FTase-FPP, ternary complex FTase-FPP-peptide, and product complex FTase-product. Relatively small-scale events such as substrate binding or product formation cause minor changes at the neighboring residues and corresponding helices, but ultimately induce much more dramatic effects on the more external regions of the enzyme
-
the isoprenoid moiety of farnsyl diphophate binds in an extended conformation in a hydrophobic cavity of the beta-subunit of the enzyme, and the diphosphate moiety binds to a positively charged cleft at the top of this cavity near the subunit interface
-
two crystal structures of enzyme complex: one containing farnesylated Ras peptide product alone and a complex that contains both the farnesylated peptide and an additional farnesyl diphosphate substrate
-
X-ray crystal structure, modelling indicates that geranylgeranyl diphosphate adopts a different conformation than the farnesyl chain of farnesyl diphosphate
-
complex of enzyme with (E,E)-[alpha,beta(n)-32P]-8-O-(3-benzoylbenzyl)-3,7-dimethyl-2,6-octadiene 1-diphosphate and of the enzyme with geranylgeranyl diphosphate
-