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PDBsum entry 1fpp
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Prenyltransferase
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PDB id
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1fpp
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Protein farnesyltransferase: structure and implications for substrate binding.
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Authors
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P.Dunten,
U.Kammlott,
R.Crowther,
D.Weber,
R.Palermo,
J.Birktoft.
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Ref.
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Biochemistry, 1998,
37,
7907-7912.
[DOI no: ]
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PubMed id
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Abstract
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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.
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