2h6g

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[[Image:2h6g.gif|left|200px]]<br /><applet load="2h6g" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2h6g.gif|left|200px]]
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caption="2h6g, resolution 1.85&Aring;" />
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'''W102T Protein Farnesyltransferase Mutant Complexed with a Geranylgeranylated DDPTASACVLS Peptide Product at 1.85A Resolution'''<br />
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{{Structure
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|PDB= 2h6g |SIZE=350|CAPTION= <scene name='initialview01'>2h6g</scene>, resolution 1.85&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=SUC:SUCROSE'>SUC</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> and <scene name='pdbligand=GER:GERAN-8-YL GERAN'>GER</scene>
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|ACTIVITY= [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]
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|GENE= Human FTase alpha subunit ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]), Human FTase beta subunit ([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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'''W102T Protein Farnesyltransferase Mutant Complexed with a Geranylgeranylated DDPTASACVLS Peptide Product at 1.85A Resolution'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2H6G is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=SUC:'>SUC</scene>, <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=GER:'>GER</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H6G OCA].
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2H6G is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H6G OCA].
==Reference==
==Reference==
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Conversion of protein farnesyltransferase to a geranylgeranyltransferase., Terry KL, Casey PJ, Beese LS, Biochemistry. 2006 Aug 15;45(32):9746-55. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16893176 16893176]
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Conversion of protein farnesyltransferase to a geranylgeranyltransferase., Terry KL, Casey PJ, Beese LS, Biochemistry. 2006 Aug 15;45(32):9746-55. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16893176 16893176]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: prenylation]]
[[Category: prenylation]]
[[Category: prenyltransferase]]
[[Category: prenyltransferase]]
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[[Category: ras]]
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[[Category: ra]]
[[Category: substrate selectivity]]
[[Category: substrate selectivity]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:38:39 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:13:11 2008''

Revision as of 15:13, 20 March 2008


PDB ID 2h6g

Drag the structure with the mouse to rotate
, resolution 1.85Å
Ligands: , and
Gene: Human FTase alpha subunit (Homo sapiens), Human FTase beta subunit (Homo sapiens)
Activity: Protein farnesyltransferase, with EC number 2.5.1.58
Coordinates: save as pdb, mmCIF, xml



W102T Protein Farnesyltransferase Mutant Complexed with a Geranylgeranylated DDPTASACVLS Peptide Product at 1.85A 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

2H6G 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 Thu Mar 20 17:13:11 2008

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