1FPP

PROTEIN FARNESYLTRANSFERASE COMPLEX WITH FARNESYL DIPHOSPHATE

Summary for 1FPP

• Entry DOI: 10.2210/pdb1fpp/pdb
• Descriptor: PROTEIN FARNESYLTRANSFERASE, ZINC ION, PHOSPHATE ION, ... (6 entities in total)
• Functional Keywords: prenyltransferase, membrane localization, heterodimer, zinc
• Biological source: Rattus norvegicus (Norway rat); More
• Total number of polymer chains: 2
• Total formula weight: 93363.13

Authors

Dunten, P.,Kammlott, U.,Crowther, R.,Weber, D.,Palermo, R.,Birktoft, J. (deposition date: 1998-07-10, release date: 1999-06-08, Last modification date: 2024-02-07)

Primary citation

Dunten, P.,Kammlott, U.,Crowther, R.,Weber, D.,Palermo, R.,Birktoft, J.
Protein farnesyltransferase: structure and implications for substrate binding.
Biochemistry, 37:7907-7912, 1998

PubMed Abstract: 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 are based in part on the observation of electron density in the active site which can be modeled as bound farnesyl diphosphate carried through the enzyme purification. In addition, our model explains in structural terms the results of mutational studies which have identified several residues critical for substrate specificity and catalysis.

PubMed: 9609683
DOI: 10.1021/bi980531o

Experimental method

X-RAY DIFFRACTION (2.75 Å)