1kzo

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[[Image:1kzo.jpg|left|200px]]<br /><applet load="1kzo" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1kzo.jpg|left|200px]]
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caption="1kzo, resolution 2.20&Aring;" />
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'''PROTEIN FARNESYLTRANSFERASE COMPLEXED WITH FARNESYLATED K-RAS4B PEPTIDE PRODUCT AND FARNESYL DIPHOSPHATE SUBSTRATE BOUND SIMULTANEOUSLY'''<br />
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{{Structure
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|PDB= 1kzo |SIZE=350|CAPTION= <scene name='initialview01'>1kzo</scene>, resolution 2.20&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=FAR:FARNESYL'>FAR</scene>, <scene name='pdbligand=FPP:FARNESYL+DIPHOSPHATE'>FPP</scene> and <scene name='pdbligand=ACY:ACETIC ACID'>ACY</scene>
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|ACTIVITY= [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]
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|GENE=
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}}
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'''PROTEIN FARNESYLTRANSFERASE COMPLEXED WITH FARNESYLATED K-RAS4B PEPTIDE PRODUCT AND FARNESYL DIPHOSPHATE SUBSTRATE BOUND SIMULTANEOUSLY'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1KZO is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with <scene name='pdbligand=ZN:'>ZN</scene>, <scene name='pdbligand=FAR:'>FAR</scene>, <scene name='pdbligand=FPP:'>FPP</scene> and <scene name='pdbligand=ACY:'>ACY</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KZO OCA].
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1KZO is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KZO OCA].
==Reference==
==Reference==
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Reaction path of protein farnesyltransferase at atomic resolution., Long SB, Casey PJ, Beese LS, Nature. 2002 Oct 10;419(6907):645-50. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12374986 12374986]
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Reaction path of protein farnesyltransferase at atomic resolution., Long SB, Casey PJ, Beese LS, Nature. 2002 Oct 10;419(6907):645-50. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12374986 12374986]
[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
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[[Category: pftase]]
[[Category: pftase]]
[[Category: product]]
[[Category: product]]
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[[Category: ras]]
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[[Category: ra]]
[[Category: substrate]]
[[Category: substrate]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:39:40 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:24:24 2008''

Revision as of 10:24, 20 March 2008

Image:1kzo.jpg


PDB ID 1kzo

Drag the structure with the mouse to rotate
, resolution 2.20Å
Ligands: , , and
Activity: Squalene synthase, with EC number 2.5.1.21
Coordinates: save as pdb, mmCIF, xml



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 Thu Mar 20 12:24:24 2008

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