1fpp
From Proteopedia
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==Overview== | ==Overview== | ||
| - | The rat protein farnesyltransferase crystal structure has been solved by | + | 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. |
==About this Structure== | ==About this Structure== | ||
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[[Category: zinc]] | [[Category: zinc]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:41:14 2008'' |
Revision as of 10:41, 21 February 2008
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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 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.
About this Structure
1FPP is a Protein complex structure of sequences from Rattus norvegicus with , and as ligands. Known structural/functional Site: . 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
Page seeded by OCA on Thu Feb 21 12:41:14 2008
Categories: Protein complex | Rattus norvegicus | Birktoft, J. | Crowther, R. | Dunten, P. | Kammlott, U. | Palermo, R. | Weber, D. | FPP | PO4 | ZN | Heterodimer | Membrane localization | Prenyltransferase | Zinc
