2H6F

Protein Farnesyltransferase Complexed with a Farnesylated DDPTASACVLS Peptide Product at 1.5A Resolution

2H6F の概要

• エントリーDOI: 10.2210/pdb2h6f/pdb
• 関連するPDBエントリー: 1FPP 1JCQ 1KZP 1N4R 1TN8 2H6G 2H6H 2H6I
• 関連するBIRD辞書のPRD_ID: PRD_900003
• 分子名称: Protein farnesyltransferase/geranylgeranyltransferase type I alpha subunit, Protein farnesyltransferase beta subunit, farnesylated peptide, ... (8 entities in total)
• 機能のキーワード: ftase, farnesyltransferase, farnesyl transferase, prenyltransferase, caax, ras, lipid modification, prenylation, substrate selectivity, transferase
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 95679.73

構造登録者

Terry, K.L.,Beese, L.S. (登録日: 2006-05-31, 公開日: 2006-08-29, 最終更新日: 2024-11-20)

主引用文献

Terry, K.L.,Casey, P.J.,Beese, L.S.
Conversion of protein farnesyltransferase to a geranylgeranyltransferase.
Biochemistry, 45:9746-9755, 2006

PubMed Abstract: 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).

PubMed: 16893176
DOI: 10.1021/bi060295e

実験手法

X-RAY DIFFRACTION (1.5 Å)