1qbq

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spinqualitylabelsall models 1qbq, resolution 2.4Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

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

Overview

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.

About this Structure

1QBQ is a Protein complex structure of sequences from Rattus norvegicus with ZN, ACT, ACE and HFP as ligands. Full crystallographic information is available from OCA.

Reference

Crystal structure of farnesyl protein transferase complexed with a CaaX peptide and farnesyl diphosphate analogue., Strickland CL, Windsor WT, Syto R, Wang L, Bond R, Wu Z, Schwartz J, Le HV, Beese LS, Weber PC, Biochemistry. 1998 Nov 24;37(47):16601-11. PMID:9843427

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