2h6h
From Proteopedia
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| , resolution 1.80Å | |||||||
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| Ligands: | , , and | ||||||
| Gene: | Human FTase alpha subunit (Homo sapiens), Human FTase beta subunit (Homo sapiens) | ||||||
| Activity: | Protein farnesyltransferase, with EC number 2.5.1.58 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Y365F Protein Farnesyltransferase Mutant Complexed with a Farnesylated DDPTASACVLS Peptide Product at 1.8A
Overview
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).
About this Structure
2H6H is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Conversion of protein farnesyltransferase to a geranylgeranyltransferase., Terry KL, Casey PJ, Beese LS, Biochemistry. 2006 Aug 15;45(32):9746-55. PMID:16893176
Page seeded by OCA on Thu Mar 20 17:13:16 2008
