1kzo

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[[Image:1kzo.jpg|left|200px]]
[[Image:1kzo.jpg|left|200px]]
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{{Structure
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<!--
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|PDB= 1kzo |SIZE=350|CAPTION= <scene name='initialview01'>1kzo</scene>, resolution 2.20&Aring;
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The line below this paragraph, containing "STRUCTURE_1kzo", creates the "Structure Box" on the page.
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|SITE=
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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=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=FAR:FARNESYL'>FAR</scene>, <scene name='pdbligand=FPP:FARNESYL+DIPHOSPHATE'>FPP</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= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Squalene_synthase Squalene synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.21 2.5.1.21] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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-->
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|DOMAIN=
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{{STRUCTURE_1kzo| PDB=1kzo | SCENE= }}
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|RELATEDENTRY=[[1kzp|1kzp]], [[1d8d|1D8D]], [[1ft1|1FT1]], [[1ft2|1FT2]], [[1kzr|1kzr]], [[1jcq|1JCQ]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1kzo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kzo OCA], [http://www.ebi.ac.uk/pdbsum/1kzo PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1kzo RCSB]</span>
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}}
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'''PROTEIN FARNESYLTRANSFERASE COMPLEXED WITH FARNESYLATED K-RAS4B PEPTIDE PRODUCT AND FARNESYL DIPHOSPHATE SUBSTRATE BOUND SIMULTANEOUSLY'''
'''PROTEIN FARNESYLTRANSFERASE COMPLEXED WITH FARNESYLATED K-RAS4B PEPTIDE PRODUCT AND FARNESYL DIPHOSPHATE SUBSTRATE BOUND SIMULTANEOUSLY'''
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[[Category: Casey, P J.]]
[[Category: Casey, P J.]]
[[Category: Long, S B.]]
[[Category: Long, S B.]]
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[[Category: caax]]
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[[Category: Caax]]
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[[Category: cancer]]
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[[Category: Cancer]]
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[[Category: farnesyl protein transferase]]
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[[Category: Farnesyl protein transferase]]
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[[Category: farnesyl transferase]]
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[[Category: Farnesyl transferase]]
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[[Category: farnesyltransferase]]
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[[Category: Farnesyltransferase]]
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[[Category: fpt]]
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[[Category: Fpt]]
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[[Category: ft]]
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[[Category: Ft]]
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[[Category: ftase]]
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[[Category: Ftase]]
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[[Category: pft]]
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[[Category: Pft]]
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[[Category: pftase]]
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[[Category: Pftase]]
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[[Category: product]]
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[[Category: Product]]
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[[Category: ra]]
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[[Category: Ra]]
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[[Category: substrate]]
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[[Category: Substrate]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 23:22:13 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:55:59 2008''
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Revision as of 20:22, 2 May 2008

Image:1kzo.jpg

Template:STRUCTURE 1kzo

PROTEIN FARNESYLTRANSFERASE COMPLEXED WITH FARNESYLATED K-RAS4B PEPTIDE PRODUCT AND FARNESYL DIPHOSPHATE SUBSTRATE BOUND SIMULTANEOUSLY


Overview

Protein farnesyltransferase (FTase) catalyses the attachment of a farnesyl lipid group to numerous essential signal transduction proteins, including members of the Ras superfamily. The farnesylation of Ras oncoproteins, which are associated with 30% of human cancers, is essential for their transforming activity. FTase inhibitors are currently in clinical trials for the treatment of cancer. Here we present a complete series of structures representing the major steps along the reaction coordinate of this enzyme. From these observations can be deduced the determinants of substrate specificity and an unusual mechanism in which product release requires binding of substrate, analogous to classically processive enzymes. A structural model for the transition state consistent with previous mechanistic studies was also constructed. The processive nature of the reaction suggests the structural basis for the successive addition of two prenyl groups to Rab proteins by the homologous enzyme geranylgeranyltransferase type-II. Finally, known FTase inhibitors seem to differ in their mechanism of inhibiting the enzyme.

About this Structure

1KZO is a Protein complex structure of sequences from Rattus norvegicus. Full crystallographic information is available from OCA.

Reference

Reaction path of protein farnesyltransferase at atomic resolution., Long SB, Casey PJ, Beese LS, Nature. 2002 Oct 10;419(6907):645-50. PMID:12374986 Page seeded by OCA on Fri May 2 23:22:13 2008

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