1fpp

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[[Image:1fpp.gif|left|200px]]
[[Image:1fpp.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1fpp |SIZE=350|CAPTION= <scene name='initialview01'>1fpp</scene>, resolution 2.75&Aring;
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The line below this paragraph, containing "STRUCTURE_1fpp", creates the "Structure Box" on the page.
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|SITE= <scene name='pdbsite=ZN:Active-Site+Zn'>ZN</scene>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=FPP:FARNESYL+DIPHOSPHATE'>FPP</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY=
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or leave the SCENE parameter empty for the default display.
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|GENE= FNTA, FNTB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus])
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-->
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|DOMAIN=
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{{STRUCTURE_1fpp| PDB=1fpp | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1fpp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fpp OCA], [http://www.ebi.ac.uk/pdbsum/1fpp PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1fpp RCSB]</span>
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}}
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'''PROTEIN FARNESYLTRANSFERASE COMPLEX WITH FARNESYL DIPHOSPHATE'''
'''PROTEIN FARNESYLTRANSFERASE COMPLEX WITH FARNESYL DIPHOSPHATE'''
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[[Category: Palermo, R.]]
[[Category: Palermo, R.]]
[[Category: Weber, D.]]
[[Category: Weber, D.]]
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[[Category: heterodimer]]
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[[Category: Heterodimer]]
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[[Category: membrane localization]]
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[[Category: Membrane localization]]
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[[Category: prenyltransferase]]
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[[Category: Prenyltransferase]]
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[[Category: zinc]]
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[[Category: Zinc]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:37:05 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:27:42 2008''
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Revision as of 13:37, 2 May 2008

Template:STRUCTURE 1fpp

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. 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 Fri May 2 16:37:05 2008

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