Farnesyltransferase - Revision history

Michal Harel at 08:47, 26 June 2019

Michal Harel — Wed, 26 Jun 2019 08:47:07 GMT

←Older revision		Revision as of 08:47, 26 June 2019
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	</StructureSection>		</StructureSection>
-	==3D structures of farnesyltransferase==

-	Updated on {{REVISIONDAY2}}-{{MONTHNAME\|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
-	{{#tree:id=OrganizedByTopic\|openlevels=0\|
-
-	*FTase
-
-	**[[1ft1]] – rFTase – rat<br />
-	**[[3q73]] – CnFTase – ''Cryptococcus neoformans''
-
-	*FTase binary complex with FPP
-
-	**[[1ft2]], [[1fpp]] – rFTase + FPP<BR />
-	**[[1o1r]], [[1o1s]], [[3ksl]], [[3ksq]] - rFTase + FPP-analog<br />
-
-	*FTase binary complex with peptide
-
-	**[[1kzp]], [[1o1t]] - rFTase + farnesylated peptide<br />
-	**[[2h6f]] - hFTase + farnesylated peptide<br />
-	**[[2h6g]], [[2h6h]], [[2h6i]] - hFTase α subunit + β subunit (mutant) + farnesylated peptide<br />
-	**[[3q79]] - CnFTase + farnesylated peptide
-
-	*FTase binary complex with inhibitor
-
-	**[[3eu5]] – rFTase + biotin-GPP<br />
-	**[[3euv]] - rFTase α subunit + β subunit (mutant)+ biotin-GPP<br />
-	**[[1n94]], [[1n95]], [[1n9a]], [[1o5m]], [[1ni1]], [[1x81]], [[2bed]], [[2r2l]] - rFTase + inhibitor<br />
-	**[[1nl4]] - rFTase α subunit (mutant) + β subunit + inhibitor
-
-	*FTase ternary complex with FPP and peptide
-
-	**[[1d8d]], [[1tn8]] - rFTase + Ras peptide + FPP-analog<br />
-	**[[1kzo]] - rFTase + farnesylated Ras peptide + FPP<BR />
-	**[[1tn7]], [[3dpy]] - rFTase + peptide + FPP-analog<BR />
-	**[[1jcr]], [[1jcs]] - rFTase + tetrapeptide inhibitor + FPP<BR />
-	**[[1d8e]] - rFTase no Zn + Ras peptide + FPP-analog<br />
-	**[[1tn6]] - hFTase + Rap2a peptide + FPP-analog<br />
-	**[[3q75]], [[3q78]] - CnFTase + peptide + FPP-analog<br />
-	**[[4l9p]] - AfFTase + peptide + FPP-analog – ''Apergillus fumigatus''<br />
-
-	*FTase ternary complex with FPP and inhibitor
-
-	**[[1sa5]], [[3e30]], [[3e32]], [[3e33]], [[3e34]], [[3e37]] - rFTase + inhibitor + FPP<BR />
-	**[[4gtm]], [[4gto]], [[4gtp]], [[4gtq]], [[4gtr]] - rFTase α subunit + β subunit + inhibitor + FPP<br />
-	**[[2zir]], [[2zis]] - rFTase α subunit (mutant) + β subunit + inhibitor + FPP<BR />
-	**[[1jcq]] – hFTase α subunit (mutant) + β subunit + inhibitor + FPP– human<br />
-	**[[1ld7]], [[1ld8]], [[1mzc]], [[1sa4]], [[1s63]], [[2f0y]] - hFTase + inhibitor + FPP<BR />
-	**[[2iej]] - hFTase + inhibitor + FPP-analog<br />
-	**[[3pz4]] - FTase + inhibitor + FPP – mouse<br />
-	**[[3q7a]], [[3q7f]] - CnFTase + inhibitor + FPP<BR />
-	**[[3fsx]], [[3sfy]] - CnFTase + inhibitor + FPP-analog<br />
-	**[[3sfx]] - CnFTase α subunit + β subunit + inhibitor + FPP<br />
-	**[[4lnb]], [[4lng]], [[4mbg]] - AfFTase (mutant) + inhibitor + FPP<br />
-
-	*FTase ternary complex with GPP and protein
-
-	**[[1n4p]], [[1n4r]], [[1n4s]] - rFTase α subunit + GTase β subunit + transforming protein + GPP<br />
-	}}
	== References ==		== References ==
	<references/>		<references/>

	[[Category:Topic Page]]		[[Category:Topic Page]]

Michal Harel at 08:46, 26 June 2019

Michal Harel — Wed, 26 Jun 2019 08:46:03 GMT

←Older revision		Revision as of 08:46, 26 June 2019
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	<StructureSection load='' size='350' 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]]) '>		<StructureSection load='' size='350' 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]]) '>
		+	== Function ==

-	'''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>.
-	.	+
-		+
	== Relevance ==		== Relevance ==

Line 11:		Line 11:

	FTase are composed of 2 subunits. <scene name='48/485616/Cv/11'>α subunit</scene> is in cyan, <scene name='48/485616/Cv/12'>β subunit</scene> is in green. <scene name='48/485616/Cv/13'>CAAX peptide and ligands</scene>. The <scene name='48/485616/Cv/14'>CAAX motif and β subunit coordinate with the Zn+2 ion</scene> and the <scene name='48/485616/Cv/15'>FPP predominantly coordinates with the β subunit</scene><ref>PMID:21816822</ref>. Water molecules are shown as red spheres.		FTase are composed of 2 subunits. <scene name='48/485616/Cv/11'>α subunit</scene> is in cyan, <scene name='48/485616/Cv/12'>β subunit</scene> is in green. <scene name='48/485616/Cv/13'>CAAX peptide and ligands</scene>. The <scene name='48/485616/Cv/14'>CAAX motif and β subunit coordinate with the Zn+2 ion</scene> and the <scene name='48/485616/Cv/15'>FPP predominantly coordinates with the β subunit</scene><ref>PMID:21816822</ref>. Water molecules are shown as red spheres.
		+
		+	==3D structures of farnesyltransferase==
		+	[[Farnesyltransferase 3D structures]]
		+
	</StructureSection>		</StructureSection>
	==3D structures of farnesyltransferase==		==3D structures of farnesyltransferase==

Alexander Berchansky at 11:00, 17 March 2019

Alexander Berchansky — Sun, 17 Mar 2019 11:00:30 GMT

←Older revision		Revision as of 11:00, 17 March 2019
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	== Structural insights ==		== Structural insights ==

-	FTase are composed of 2 subunits. <scene name='48/485616/Cv/5'>α subunit</scene> is in cyan, <scene name='48/485616/Cv/4'>β subunit</scene> is in green. <scene name='48/485616/Cv/6'>CAAX peptide and ligands</scene>. The <scene name='48/485616/Cv/9'>CAAX motif and β subunit coordinate with the Zn+2 ion</scene> and the <scene name='48/485616/Cv/10'>FPP predominantly coordinates with the β subunit</scene><ref>PMID:21816822</ref>. Water molecules are shown as red spheres.	+	FTase are composed of 2 subunits. <scene name='48/485616/Cv/11'>α subunit</scene> is in cyan, <scene name='48/485616/Cv/12'>β subunit</scene> is in green. <scene name='48/485616/Cv/13'>CAAX peptide and ligands</scene>. The <scene name='48/485616/Cv/14'>CAAX motif and β subunit coordinate with the Zn+2 ion</scene> and the <scene name='48/485616/Cv/15'>FPP predominantly coordinates with the β subunit</scene><ref>PMID:21816822</ref>. Water molecules are shown as red spheres.
	</StructureSection>		</StructureSection>
	==3D structures of farnesyltransferase==		==3D structures of farnesyltransferase==

Joel L. Sussman at 10:42, 20 October 2017

Joel L. Sussman — Fri, 20 Oct 2017 10:42:28 GMT

←Older revision		Revision as of 10:42, 20 October 2017
Line 1:		Line 1:
-	<StructureSection load='~~3q75~~' size='350' 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]]) '>	+	<StructureSection load='' size='350' 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>

Michal Harel at 18:52, 19 October 2017

Michal Harel — Thu, 19 Oct 2017 18:52:26 GMT

←Older revision		Revision as of 18:52, 19 October 2017
Line 1:		Line 1:
-	<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]]) '>	+	<StructureSection load='3q75' size='350' 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>

Alexander Berchansky at 10:49, 25 January 2016

Alexander Berchansky — Mon, 25 Jan 2016 10:49:11 GMT

←Older revision		Revision as of 10:49, 25 January 2016
Line 10:		Line 10:
	== Structural insights ==		== Structural insights ==

-	FTase are composed of 2 subunits. <scene name='48/485616/Cv/5'>α subunit</scene> is in cyan, <scene name='48/485616/Cv/4'>β subunit</scene> is in green. <scene name='48/485616/Cv/6'>CAAX peptide and ligands</scene>. The <scene name='48/485616/Cv/9'>CAAX motif and β subunit coordinate with the Zn+2 ion</scene> and the <scene name='48/485616/Cv/10'>FPP predominantly coordinates with the β subunit</scene><ref>PMID:21816822</ref>.	+	FTase are composed of 2 subunits. <scene name='48/485616/Cv/5'>α subunit</scene> is in cyan, <scene name='48/485616/Cv/4'>β subunit</scene> is in green. <scene name='48/485616/Cv/6'>CAAX peptide and ligands</scene>. The <scene name='48/485616/Cv/9'>CAAX motif and β subunit coordinate with the Zn+2 ion</scene> and the <scene name='48/485616/Cv/10'>FPP predominantly coordinates with the β subunit</scene><ref>PMID:21816822</ref>. Water molecules are shown as red spheres.
	</StructureSection>		</StructureSection>
	==3D structures of farnesyltransferase==		==3D structures of farnesyltransferase==

Alexander Berchansky at 10:46, 25 January 2016

Alexander Berchansky — Mon, 25 Jan 2016 10:46:31 GMT

←Older revision		Revision as of 10:46, 25 January 2016
Line 10:		Line 10:
	== Structural insights ==		== Structural insights ==

-	FTase are composed of 2 subunits. <scene name='48/485616/Cv/5'>α subunit</scene> is in cyan, <scene name='48/485616/Cv/4'>β subunit</scene> is in green. <scene name='48/485616/Cv/6'>CAAX peptide and ligands</scene>. The <scene name='48/485616/Cv/9'>CAAX motif and β subunit coordinate with the Zn+2 ion</scene> and the FPP coordinates with the β subunit<ref>PMID:21816822</ref>.	+	FTase are composed of 2 subunits. <scene name='48/485616/Cv/5'>α subunit</scene> is in cyan, <scene name='48/485616/Cv/4'>β subunit</scene> is in green. <scene name='48/485616/Cv/6'>CAAX peptide and ligands</scene>. The <scene name='48/485616/Cv/9'>CAAX motif and β subunit coordinate with the Zn+2 ion</scene> and the <scene name='48/485616/Cv/10'>FPP predominantly coordinates with the β subunit</scene><ref>PMID:21816822</ref>.
	</StructureSection>		</StructureSection>
	==3D structures of farnesyltransferase==		==3D structures of farnesyltransferase==

Alexander Berchansky at 09:39, 25 January 2016

Alexander Berchansky — Mon, 25 Jan 2016 09:39:34 GMT

←Older revision		Revision as of 09:39, 25 January 2016
Line 10:		Line 10:
	== Structural insights ==		== Structural insights ==

-	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~~. <scene name='48/485616/Cv/6'>CAAX peptide and ligands</scene>. The CAAX motif ~~coordinates~~ with the Zn~~<sup>~~+2</~~sup~~> ~~ion~~ and the FPP coordinates with the β subunit<ref>PMID:21816822</ref>.	+	FTase are composed of 2 subunits. <scene name='48/485616/Cv/5'>α subunit</scene> is in cyan, <scene name='48/485616/Cv/4'>β subunit</scene> is in green. <scene name='48/485616/Cv/6'>CAAX peptide and ligands</scene>. The <scene name='48/485616/Cv/9'>CAAX motif and β subunit coordinate with the Zn+2 ion</scene> and the FPP coordinates with the β subunit<ref>PMID:21816822</ref>.
	</StructureSection>		</StructureSection>
	==3D structures of farnesyltransferase==		==3D structures of farnesyltransferase==

Alexander Berchansky at 09:10, 25 January 2016

Alexander Berchansky — Mon, 25 Jan 2016 09:10:40 GMT

←Older revision		Revision as of 09:10, 25 January 2016
Line 10:		Line 10:
	== Structural insights ==		== Structural insights ==

-	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>.	+	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. <scene name='48/485616/Cv/6'>CAAX peptide and ligands</scene>. 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==

Alexander Berchansky at 09:03, 25 January 2016

Alexander Berchansky — Mon, 25 Jan 2016 09:03:12 GMT

←Older revision		Revision as of 09:03, 25 January 2016
Line 1:		Line 1:
-	<StructureSection load='3q75' size='~~350~~' side='right' scene='48/485616/Cv/1' 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 ~~(pink)~~ (PDB code [[3q75]]) '>	+	<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>
Line 10:		Line 10:
	== Structural insights ==		== Structural insights ==

-	FTase are composed of 2 subunits. The β subunit 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>.	+	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==