2H6G: W102t Protein Farnesyltransferase Mutant Complexed With A Geranylgeranylated Ddptasacvls Peptide Product At 1.85a Resolution

Posttranslational modifications are essential for the proper function of a number of proteins in the cell. One such modification, the covalent attachment of a single isoprenoid lipid (prenylation), is carried out by the CaaX prenyltransferases, protein farnesyltransferase (FTase) and protein geranylgeranyltransferase type-I (GGTase-I). Substrate proteins of these two enzymes are involved in a variety of cellular functions but are largely associated with signal transduction. These modified proteins include members of the Ras superfamily, heterotrimeric G-proteins, centromeric proteins, and a number of proteins involved in nuclear integrity. Although FTase and GGTase-I are highly homologous, they are quite selective for their substrates, particularly for their isoprenoid diphosphate substrates, FPP and GGPP, respectively. Here, we present both crystallographic and kinetic analyses of mutants designed to explore this isoprenoid specificity and demonstrate that this specificity is dependent upon two enzyme residues in the beta subunits of the enzymes, W102beta and Y365beta in FTase (T49beta and F324beta, respectively, in GGTase-I).
PDB ID: 2H6GDownload
MMDB ID: 40988
PDB Deposition Date: 2006/5/31
Updated in MMDB: 2010/10
Experimental Method:
x-ray diffraction
Resolution: 1.85  Å
Source Organism:
synthetic construct
Similar Structures:
Biological Unit for 2H6G: trimeric; determined by author and by software (PISA)
Molecular Components in 2H6G
Label Count Molecule
Proteins (3 molecules)
Protein Farnesyltransferase/geranylgeranyltransferase Type I Alpha Subunit(Gene symbol: FNTA)
Molecule annotation
Protein Farnesyltransferase Beta Subunit(Gene symbol: FNTB)
Molecule annotation
Farnesylated Peptide
Molecule annotation
Chemicals (3 molecules)
* Click molecule labels to explore molecular sequence information.

Citing MMDB