2h6f

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[[Image:2h6f.gif|left|200px]]
[[Image:2h6f.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 2h6f |SIZE=350|CAPTION= <scene name='initialview01'>2h6f</scene>, resolution 1.5&Aring;
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The line below this paragraph, containing "STRUCTURE_2h6f", 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=SUC:SUCROSE'>SUC</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/Protein_farnesyltransferase Protein farnesyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.58 2.5.1.58] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE= FNTA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]), FNTB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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-->
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|DOMAIN=
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{{STRUCTURE_2h6f| PDB=2h6f | SCENE= }}
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|RELATEDENTRY=[[1kzp|1KZP]], [[1n4r|1N4R]], [[1tn8|1TN8]], [[1jcq|1JCQ]], [[1fpp|1FPP]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2h6f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h6f OCA], [http://www.ebi.ac.uk/pdbsum/2h6f PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2h6f RCSB]</span>
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}}
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'''Protein Farnesyltransferase Complexed with a Farnesylated DDPTASACVLS Peptide Product at 1.5A Resolution'''
'''Protein Farnesyltransferase Complexed with a Farnesylated DDPTASACVLS Peptide Product at 1.5A Resolution'''
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[[Category: Beese, L S.]]
[[Category: Beese, L S.]]
[[Category: Terry, K L.]]
[[Category: Terry, K L.]]
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[[Category: caax]]
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[[Category: Caax]]
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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: ftase]]
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[[Category: Ftase]]
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[[Category: lipid modification]]
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[[Category: Lipid modification]]
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[[Category: prenylation]]
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[[Category: Prenylation]]
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[[Category: prenyltransferase]]
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[[Category: Prenyltransferase]]
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[[Category: ra]]
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[[Category: Ra]]
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[[Category: substrate selectivity]]
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[[Category: Substrate selectivity]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 05:55:19 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:26:07 2008''
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Revision as of 02:55, 4 May 2008

Template:STRUCTURE 2h6f

Protein Farnesyltransferase Complexed with a Farnesylated DDPTASACVLS Peptide Product at 1.5A Resolution


Overview

Posttranslational modifications are essential for the proper function of a number of proteins in the cell. One such modification, the covalent attachment of a single isoprenoid lipid (prenylation), is carried out by the CaaX prenyltransferases, protein farnesyltransferase (FTase) and protein geranylgeranyltransferase type-I (GGTase-I). Substrate proteins of these two enzymes are involved in a variety of cellular functions but are largely associated with signal transduction. These modified proteins include members of the Ras superfamily, heterotrimeric G-proteins, centromeric proteins, and a number of proteins involved in nuclear integrity. Although FTase and GGTase-I are highly homologous, they are quite selective for their substrates, particularly for their isoprenoid diphosphate substrates, FPP and GGPP, respectively. Here, we present both crystallographic and kinetic analyses of mutants designed to explore this isoprenoid specificity and demonstrate that this specificity is dependent upon two enzyme residues in the beta subunits of the enzymes, W102beta and Y365beta in FTase (T49beta and F324beta, respectively, in GGTase-I).

About this Structure

2H6F is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Conversion of protein farnesyltransferase to a geranylgeranyltransferase., Terry KL, Casey PJ, Beese LS, Biochemistry. 2006 Aug 15;45(32):9746-55. PMID:16893176 Page seeded by OCA on Sun May 4 05:55:19 2008

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