2h6f
From Proteopedia
(New page: 200px<br /> <applet load="2h6f" size="450" color="white" frame="true" align="right" spinBox="true" caption="2h6f, resolution 1.5Å" /> '''Protein Farnesyltran...) |
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caption="2h6f, resolution 1.5Å" /> | caption="2h6f, resolution 1.5Å" /> | ||
'''Protein Farnesyltransferase Complexed with a Farnesylated DDPTASACVLS Peptide Product at 1.5A Resolution'''<br /> | '''Protein Farnesyltransferase Complexed with a Farnesylated DDPTASACVLS Peptide Product at 1.5A Resolution'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2H6F 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 SUC, ZN, FAR and ACY 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:// | + | 2H6F 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>, <scene name='pdbligand=FAR:'>FAR</scene> and <scene name='pdbligand=ACY:'>ACY</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=2H6F OCA]. |
==Reference== | ==Reference== | ||
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[[Category: substrate selectivity]] | [[Category: substrate selectivity]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 17:30:06 2008'' |
Revision as of 15:30, 15 February 2008
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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 with , , and as ligands. Active as Protein farnesyltransferase, with EC number 2.5.1.58 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
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