1QBQ

STRUCTURE OF RAT FARNESYL PROTEIN TRANSFERASE COMPLEXED WITH A CVIM PEPTIDE AND ALPHA-HYDROXYFARNESYLPHOSPHONIC ACID.

1QBQ の概要

• エントリーDOI: 10.2210/pdb1qbq/pdb
• 関連するPDBエントリー: 1FPP 1FT1 1FT2
• 分子名称: FPT ALPHA-SUBUNIT, FPT BETA-SUBUNIT, ACETYL-CYS-VAL-ILE-SELENOMET-COOH PEPTIDE, ... (7 entities in total)
• 機能のキーワード: alpha-alpha-barrel helical crescent, transferase
• 由来する生物種: Rattus norvegicus (Norway rat); 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 89453.21

構造登録者

Strickland, C.L.,Windsor, W.T.,Syto, R.,Wang, L.,Bond, R.,Wu, Z.,Schwartz, J.,Le, H.V.,Beese, L.S.,Weber, P.C. (登録日: 1999-04-27, 公開日: 1999-06-18, 最終更新日: 2024-10-16)

主引用文献

Strickland, C.L.,Windsor, W.T.,Syto, R.,Wang, L.,Bond, R.,Wu, Z.,Schwartz, J.,Le, H.V.,Beese, L.S.,Weber, P.C.
Crystal structure of farnesyl protein transferase complexed with a CaaX peptide and farnesyl diphosphate analogue
Biochemistry, 37:16601-16611, 1998

PubMed Abstract: The crystallographic structure of acetyl-Cys-Val-Ile-selenoMet-COOH and alpha-hydroxyfarnesylphosphonic acid (alphaHFP) complexed with rat farnesyl protein transferase (FPT) (space group P61, a = b = 174. 13 A, c = 69.71 A, alpha = beta = 90 degrees, gamma = 120 degrees, Rfactor = 21.8%, Rfree = 29.2%, 2.5 A resolution) is reported. In the ternary complex, the bound substrates are within van der Waals contact of each other and the FPT enzyme. alphaHFP binds in an extended conformation in the active-site cavity where positively charged side chains and solvent molecules interact with the phosphate moiety and aromatic side chains pack adjacent to the isoprenoid chain. The backbone of the bound CaaX peptide adopts an extended conformation, and the side chains interact with both FPT and alphaHFP. The cysteine sulfur of the bound peptide coordinates the active-site zinc. Overall, peptide binding and recognition appear to be dominated by side-chain interactions. Comparison of the structures of the ternary complex and unliganded FPT [Park, H., Boduluri, S., Moomaw, J., Casey, P., and Beese, L. (1997) Science 275, 1800-1804] shows that major rearrangements of several active site side chains occur upon substrate binding.

PubMed: 9843427
DOI: 10.1021/bi981197z

実験手法

X-RAY DIFFRACTION (2.4 Å)