Farnesyltransferase
From Proteopedia
(Difference between revisions)
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- | <StructureSection load='3q75' size=' | + | <StructureSection load='3q75' size='450' side='right' scene='48/485616/Cv/2' caption=' Farnesyltransferase α subunit (cyan) and β subunit (green) complex with farnesyl diphosphate (FPP) analog, Zn+2 ion (grey), sulfonic acid derivative and CAAX peptide (PDB code [[3q75]]) '> |
'''Farnesyltransferase''' (FTase) is part of the prenyltransferase group. FTase modifies proteins by adding farnesyl diphosphate (FPP) – an isoprenoid lipid – to a cysteine in a CAAX motif near the C terminal. This addition forms a thioether linkage, makes the protein more hydrophobic and associates it with the membrane. Farnesylated proteins – like those of the Ras family - are involved in cellular signaling<ref>PMID:15451670</ref> | '''Farnesyltransferase''' (FTase) is part of the prenyltransferase group. FTase modifies proteins by adding farnesyl diphosphate (FPP) – an isoprenoid lipid – to a cysteine in a CAAX motif near the C terminal. This addition forms a thioether linkage, makes the protein more hydrophobic and associates it with the membrane. Farnesylated proteins – like those of the Ras family - are involved in cellular signaling<ref>PMID:15451670</ref> | ||
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== Structural insights == | == Structural insights == | ||
- | FTase are composed of 2 subunits. | + | FTase are composed of 2 subunits. <scene name='48/485616/Cv/5'>α subunit</scene> is in cyan. The <scene name='48/485616/Cv/4'>β subunit</scene> coordinates a Zn atom. The CAAX motif coordinates with the Zn<sup>+2</sup> ion and the FPP coordinates with the β subunit<ref>PMID:21816822</ref>. |
</StructureSection> | </StructureSection> | ||
==3D structures of farnesyltransferase== | ==3D structures of farnesyltransferase== |
Revision as of 09:03, 25 January 2016
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3D structures of farnesyltransferase
Updated on 25-January-2016
References
- ↑ Reid TS, Terry KL, Casey PJ, Beese LS. Crystallographic analysis of CaaX prenyltransferases complexed with substrates defines rules of protein substrate selectivity. J Mol Biol. 2004 Oct 15;343(2):417-33. PMID:15451670 doi:10.1016/j.jmb.2004.08.056
- ↑ Hast MA, Nichols CB, Armstrong SM, Kelly SM, Hellinga HW, Alspaugh JA, Beese LS. Structures of Cryptococcus neoformans Protein Farnesyltransferase Reveal Strategies for Developing Inhibitors That Target Fungal Pathogens. J Biol Chem. 2011 Oct 7;286(40):35149-62. Epub 2011 Aug 4. PMID:21816822 doi:10.1074/jbc.M111.250506