1fpp

From Proteopedia

Revision as of 13:07, 30 October 2007

PROTEIN FARNESYLTRANSFERASE COMPLEX WITH FARNESYL DIPHOSPHATE

Overview

The rat protein farnesyltransferase crystal structure has been solved by, multiple isomorphous replacement methods at a resolution of 2.75 A. The, three-dimensional structure, together with recent data on the effects of, several mutations, led us to propose a model for substrate binding which, differs from the model presented by Park et al. based on their independent, structure determination [Park, H. -W., Boduluri, S. R., Moomaw, J. F., Casey, P. J., and Beese, L. S. (1997) Science 275, 1800-1804]. Both, farnesyl diphosphate and peptide substrates can be accommodated in the, hydrophobic active-site barrel, with the sole charged residue inside the, barrel, Arg202 of the beta-subunit, forming a salt bridge with the, negatively charged carboxy terminus of peptide substrates. Our proposals, ... [(full description)]

About this Structure

1FPP is a [Protein complex] structure of sequences from [Rattus norvegicus] with ZN, PO4 and FPP as [ligands]. Structure known Active Site: ZN. Full crystallographic information is available from [OCA].

Reference

Protein farnesyltransferase: structure and implications for substrate binding., Dunten P, Kammlott U, Crowther R, Weber D, Palermo R, Birktoft J, Biochemistry. 1998 Jun 2;37(22):7907-12. PMID:9609683

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