Histone acetyltransferase - Revision history

Michal Harel at 07:30, 11 February 2021

Michal Harel — Thu, 11 Feb 2021 07:30:16 GMT

←Older revision		Revision as of 07:30, 11 February 2021
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	'''Histone acetyltransferase''' (HAT) catalyzes the acetylation of lysine residues on histone proteins. The acetyl group is transferred from acetyl-CoA to form ε-N-acetyl lysine. HAT contains a bromodomain – a ca. 110 amino acids domain which binds acetylated lysine. Histone acetylation is linked to transcription activation<ref>PMID:11395403</ref>.		'''Histone acetyltransferase''' (HAT) catalyzes the acetylation of lysine residues on histone proteins. The acetyl group is transferred from acetyl-CoA to form ε-N-acetyl lysine. HAT contains a bromodomain – a ca. 110 amino acids domain which binds acetylated lysine. Histone acetylation is linked to transcription activation<ref>PMID:11395403</ref>.

-	See also [[Histone acetyltransferase 1-2 Complex (HAT1/2)}}.	+	See also [[Histone acetyltransferase 1-2 Complex (HAT1/2)]].

	== Relevance ==		== Relevance ==

Michal Harel at 07:30, 11 February 2021

Michal Harel — Thu, 11 Feb 2021 07:30:00 GMT

←Older revision		Revision as of 07:30, 11 February 2021
Line 3:		Line 3:
	'''Histone acetyltransferase''' (HAT) catalyzes the acetylation of lysine residues on histone proteins. The acetyl group is transferred from acetyl-CoA to form ε-N-acetyl lysine. HAT contains a bromodomain – a ca. 110 amino acids domain which binds acetylated lysine. Histone acetylation is linked to transcription activation<ref>PMID:11395403</ref>.		'''Histone acetyltransferase''' (HAT) catalyzes the acetylation of lysine residues on histone proteins. The acetyl group is transferred from acetyl-CoA to form ε-N-acetyl lysine. HAT contains a bromodomain – a ca. 110 amino acids domain which binds acetylated lysine. Histone acetylation is linked to transcription activation<ref>PMID:11395403</ref>.

-	See also [[~~Hione~~ acetyltransferase 1-2 Complex (HAT1/2)}}.	+	See also [[Histone acetyltransferase 1-2 Complex (HAT1/2)}}.

	== Relevance ==		== Relevance ==

Michal Harel at 07:29, 11 February 2021

Michal Harel — Thu, 11 Feb 2021 07:29:38 GMT

←Older revision		Revision as of 07:29, 11 February 2021
Line 2:		Line 2:
	== Function ==		== Function ==
	'''Histone acetyltransferase''' (HAT) catalyzes the acetylation of lysine residues on histone proteins. The acetyl group is transferred from acetyl-CoA to form ε-N-acetyl lysine. HAT contains a bromodomain – a ca. 110 amino acids domain which binds acetylated lysine. Histone acetylation is linked to transcription activation<ref>PMID:11395403</ref>.		'''Histone acetyltransferase''' (HAT) catalyzes the acetylation of lysine residues on histone proteins. The acetyl group is transferred from acetyl-CoA to form ε-N-acetyl lysine. HAT contains a bromodomain – a ca. 110 amino acids domain which binds acetylated lysine. Histone acetylation is linked to transcription activation<ref>PMID:11395403</ref>.
		+
		+	See also [[Hione acetyltransferase 1-2 Complex (HAT1/2)}}.

	== Relevance ==		== Relevance ==

Michal Harel at 08:25, 28 July 2019

Michal Harel — Sun, 28 Jul 2019 08:25:17 GMT

←Older revision		Revision as of 08:25, 28 July 2019
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	</StructureSection>		</StructureSection>
-	== 3D Structures of histone acetyltransferase ==

-	Updated on {{REVISIONDAY2}}-{{MONTHNAME\|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
-	{{#tree:id=OrganizedByTopic\|openlevels=0\|
-
-	*Histone acetyltransferase; Human domains – HAT 170-458; catalytic 497-662; bromodomain 729-837;
-
-	**[[1f68]] – hHAT bromodomain (mutant) – human – NMR
-
-	**[[1n72]] - hHAT bromodomain – NMR
-
-	**[[3d7c]] - hHAT bromodomain
-
-	**[[3gg3]] - hHAT PCAF bromodomain
-
-	**[[2ou2]] - hHAT HTATIP<br />
-	**[[2eko]] – hHAT HTATIP histone tail-binding domain - NMR
-
-	**[[1z4r]] – hHAT catalytic domain<br />
-	**[[3toa]] - hHAT Myst1 HAT domain<br />
-	**[[3tob]] - hHAT Myst1 HAT domain (mutant)<br />
-	**[[2rc4]] – hHAT Myst3 acetyltransferase domain<br />
-	**[[5trm]] - hHAT KAT2A catalytic domain <br />
-	**[[4nsq]] - hHAT KAT2B<br />
-	**[[4qqg]] - hHAT KAT5 N terminal<br />
-	**[[2ln0]] - hHAT KAT6A<br />
-	**[[4ljn]] - hHAT KAT6A double PHD finger<br />
-	**[[5wci]] - hHAT KAT8 HAT domain <br />
-	**[[5j8c]], [[5j8f]] - hHAT KAT8 HAT domain (mutant)<br />
-	**[[1qso]] - yHAT HPA2 – yeast<br />
-	**[[3to7]] – yHAT Esa1<br />
-	**[[2rnz]] – yHAT Esa1 chromodomain – NMR
-
-	**[[2ro0]] - yHAT Esa1 knotted Tudor domain – NMR<br />
-	**[[1ygh]] – yHAT HAT domain<br />
-	**[[2qec]] – HAT HPA2 (mutant) – ''Corynebacterium glutamicum''<br />
-	**[[6ia8]], [[6iad]], [[6iaz]] - HAT – ''Methanocaldococcus infernus''<br />
-
-	*Histone acetyltransferase binary complexes
-
-	**[[1wug]], [[1wum]] – hHAT PCAF + small ligand
-
-	**[[1zs5]] – hHAT bromodomain + inhibitor – NMR
-
-	**[[2ozu]] - hHAT MYST3 catalytic domain + acetyl-CoA
-
-	**[[2p0w]] - hHAT 1 catalytic domain + histone H4 peptide
-
-	**[[2rnw]], [[2rnx]] - hHAT PCAF bromodomain + histone H3 peptide - NMR<br />
-	**[[5h84]] - hHAT KAT2A catalytic domain + propionyl CoA<br />
-	**[[5h86]] - hHAT KAT2A catalytic domain + butyryl CoA<br />
-	**[[5trl]] - hHAT KAT2A catalytic domain + succinyl CoA<br />
-	**[[5mlj]], [[6j3p]] - hHAT KAT2A bromodomain + inhibitor<br />
-	**[[5lvq]], [[5lvr]], [[5fdz]], [[5fe0]], [[5fe1]], [[5fe2]], [[5fe3]], [[5fe4]], [[5fe5]], [[5fe6]], [[5fe7]], [[5fe8]], [[5fe9]], [[5mkx]] - hHAT KAT2B bromodomain + inhibitor<br />
-	**[[4dnc]] – hHAT KAT8 HAT domain + male-specific lethal 1 homolog<br />
-	**[[3v43]], [[4lk9]], [[4lka]], [[4llb]], [[5b75]], [[5b76]], [[5b77]], [[5b78]] - hHAT KAT6A + H3.1 peptide<br />
-	**[[5u2j]] - hHAT KAT6B + H3K14BU peptide<br />
-	**[[5gk9]] - hHAT KAT7 + BRD1<br />
-	**[[5ml0]] - HAT KAT2B bromodomain + inhibitor - mouse<br />
-	**[[1bob]] – yHAT 1 + acetyl-CoA
-
-	**[[1qsm]] – yHAT HPA2 + acetyl-CoA
-
-	**[[1fy7]], [[1mja]] - yHAT Esa1 + CoA<br />
-	**[[3to6]] - yHAT Esa1 + H4 peptide<br />
-	**[[4psw]] - yHAT B + H4 peptide<br />
-	**[[1e6i]] - yHAT bromodomain + H4 peptide<br />
-	**[[1mj9]], [[3to9]] - yHAT Esa1 (mutant) + CoA
-
-	**[[1mjb]] - yHAT Esa1 (mutant) + acetyl-CoA
-
-	**[[3qm0]] - yHAT RTT109 (mutant) + acetyl-CoA
-
-	**[[3q35]], [[3q66]], [[3q68]] – yHAT RTT109 + vacuolar protein sorting-associated protein 75
-
-	**[[5gcn]] – TtHAT Gcn5 + CoA – ''Tetrahymena thermophila'' - NMR<br />
-	**[[5tpx]] - HAT GCN5 + probe – ''Plasmodium falciparum''<br />
-
-	*Histone acetyltransferase ternary complexes
-
-	**[[3q33]] – yHAT RTT109 + vacuolar protein sorting-associated protein 75 + histone H3 peptide<br />
-	**[[4psx]] - yHAT B + H3 peptide + H4 peptide<br />
-	**[[5j9q]], [[5j9t]], [[5j9u]], [[5j9w]] - yHAT Esa1 (mutant) + chromatin modification-related protein + enhancer of polycomb-like protein<br />
-	**[[6cw3]], [[6cw2]] - yHAT GCN5 residues 67-316 + transcriptional adaptor + antibody<br />
-	**[[1q2c]] - TtHAT Gcn5 + CoA + histone H4 peptide
-
-	**[[1q2d]] - TtHAT Gcn5 + CoA + p53 peptide
-
-	* Histone acetyltransferase P300; domains – core domain residues 1043-1519; bromodomain residues 1040-1161; acetyltransferase domain residues 1287-1664; TAZ2 domain 1723-1836:
-
-	**[[3i3j]] – hHAT P300 bromodomain <br />
-	**[[3io2]] – hHAT P300 TAZ2 domain <br />
-	**[[4bhw]] - hHAT P300 core (mutant)<br />
-	**[[6k4n]] - hHAT P300 bromodomain+acetyltransferase domains – Cryo EM<br />
-	**[[2mh0]] - hHAT P300 TAZ2 + transcription factor ITF-1<br />
-	**[[2mh0]], [[2k8f]] - hHAT P300 TAZ2 (mutant) + p53 peptide<br />
-	**[[4pzr]], [[4pzs]] - hHAT P300 acetyltransferase domain (mutant) + acetyl CoA<br />
-	**[[4pzt]] - hHAT P300 acetyltransferase domain (mutant) + acetonyl CoA<br />
-	**[[5lkt]] - hHAT P300 residues 1581-1666 + butyryl CoA<br />
-	**[[5lku]] - hHAT P300 core + CoA<br />
-	**[[5lkx]] - hHAT P300 core (mutant) + propionyl CoA<br />
-	**[[5lkz]] - hHAT P300 core (mutant) + crotonyl CoA<br />
-	**[[3biy]] – hHAT P300 acetyltransferase domain + lysine CoA derivative<br />
-	**[[5kj2]] - hHAT P300 acetyltransferase domain + inhibitor<br />
-	**[[6gyr]] - hHAT P300 core+acetyltransferase domains + lysine CoA derivative<br />
-	**[[5xzc]] - hHAT P300 core+acetyltransferase domains + p53<br />
-	**[[5bt3]], [[5nu5]], [[5lpk]], [[5lpm]] - hHAT P300 bromodomain + inhibitor<br />
-	**[[6gyt]] - hHAT P300 bromodomain + histone H4 peptide<br />
-	**[[3p57]] - hHAT P300 TAZ2 domain + myocyte-specific enhancer factor 2A + DNA
-	}}
	== References ==		== References ==
	<references/>		<references/>
	[[Category:Topic Page]]		[[Category:Topic Page]]

Michal Harel at 08:23, 28 July 2019

Michal Harel — Sun, 28 Jul 2019 08:23:59 GMT

←Older revision		Revision as of 08:23, 28 July 2019
Line 11:		Line 11:
	== Structural highlights ==		== Structural highlights ==
	<scene name='46/467281/Cv/7'>HAT binds acetyl CoA</scene> in a <scene name='46/467281/Cv/9'>cleft toward the center of the concave surface</scene> of the protein<ref>PMID:9727486</ref>. Water molecules shown as red spheres.		<scene name='46/467281/Cv/7'>HAT binds acetyl CoA</scene> in a <scene name='46/467281/Cv/9'>cleft toward the center of the concave surface</scene> of the protein<ref>PMID:9727486</ref>. Water molecules shown as red spheres.
		+
		+	== 3D Structures of histone acetyltransferase ==
		+	[[Histone acetyltransferase 3D structures]]
		+
	</StructureSection>		</StructureSection>
	== 3D Structures of histone acetyltransferase ==		== 3D Structures of histone acetyltransferase ==
Line 17:		Line 21:
	{{#tree:id=OrganizedByTopic\|openlevels=0\|		{{#tree:id=OrganizedByTopic\|openlevels=0\|

-	*Histone acetyltransferase; Human domains – catalytic ~~domain residues~~ 497-662; bromodomain ~~residues~~ 729-837;	+	*Histone acetyltransferase; Human domains – HAT 170-458; catalytic 497-662; bromodomain 729-837;

-	**[[1qso]] - yHAT HPA2 – yeast<br />
-	**[[3to7]] – yHAT Esa1<br />
-	**[[2rnz]] – yHAT Esa1 chromodomain – NMR
-
-	**[[2ro0]] - yHAT Esa1 knotted Tudor domain – NMR<br />
-	**[[1ygh]] – yHAT HAT domain<br />
	**[[1f68]] – hHAT bromodomain (mutant) – human – NMR		**[[1f68]] – hHAT bromodomain (mutant) – human – NMR

Line 37:		Line 35:

	**[[1z4r]] – hHAT catalytic domain<br />		**[[1z4r]] – hHAT catalytic domain<br />
-	**[[3toa]] - hHAT Myst1 ~~residues 177-447~~<br />	+	**[[3toa]] - hHAT Myst1 HAT domain<br />
-	**[[3tob]] - hHAT Myst1 ~~residues 177-447~~ (mutant)<br />	+	**[[3tob]] - hHAT Myst1 HAT domain (mutant)<br />
	**[[2rc4]] – hHAT Myst3 acetyltransferase domain<br />		**[[2rc4]] – hHAT Myst3 acetyltransferase domain<br />
	**[[5trm]] - hHAT KAT2A catalytic domain <br />		**[[5trm]] - hHAT KAT2A catalytic domain <br />
Line 45:		Line 43:
	**[[2ln0]] - hHAT KAT6A<br />		**[[2ln0]] - hHAT KAT6A<br />
	**[[4ljn]] - hHAT KAT6A double PHD finger<br />		**[[4ljn]] - hHAT KAT6A double PHD finger<br />
-	**[[5wci]] - hHAT KAT8 ~~residues 174-449~~ <br />	+	**[[5wci]] - hHAT KAT8 HAT domain <br />
-	**[[5j8c]], [[5j8f]] - hHAT KAT8 ~~residues 177-447~~ (mutant)<br />	+	**[[5j8c]], [[5j8f]] - hHAT KAT8 HAT domain (mutant)<br />
-	**[[~~2qec~~]] ~~– HAT~~ HPA2 ~~(mutant)~~ – ~~''Corynebacterium glutamicum''~~	+	**[[1qso]] - yHAT HPA2 – yeast<br />
		+	**[[3to7]] – yHAT Esa1<br />
		+	**[[2rnz]] – yHAT Esa1 chromodomain – NMR

-	*~~Histone acetyltransferase binary complexes~~	+	**[[2ro0]] - yHAT Esa1 knotted Tudor domain – NMR<br />
		+	**[[1ygh]] – yHAT HAT domain<br />
		+	**[[2qec]] – HAT HPA2 (mutant) – ''Corynebacterium glutamicum''<br />
		+	**[[6ia8]], [[6iad]], [[6iaz]] - HAT – ''Methanocaldococcus infernus''<br />

-	**[[1bob]] – yHAT 1 + acetyl-CoA	+	*Histone acetyltransferase binary complexes

-	**[[1qsm]] – yHAT HPA2 + acetyl-CoA
-
-	**[[1fy7]], [[1mja]] - yHAT Esa1 + CoA<br />
-	**[[3to6]] - yHAT Esa1 + H4 peptide<br />
-	**[[4psw]] - yHAT B + H4 peptide<br />
-	**[[1e6i]] - yHAT bromodomain + H4 peptide<br />
-	**[[1mj9]], [[3to9]] - yHAT Esa1 (mutant) + CoA
-
-	**[[1mjb]] - yHAT Esa1 (mutant) + acetyl-CoA
-
-	**[[3qm0]] - yHAT RTT109 (mutant) + acetyl-CoA
-
-	**[[3q35]], [[3q66]], [[3q68]] – yHAT RTT109 + vacuolar protein sorting-associated protein 75
-
-	**[[5gcn]] – TtHAT Gcn5 + CoA – ''Tetrahymena thermophila'' - NMR<br />
	**[[1wug]], [[1wum]] – hHAT PCAF + small ligand		**[[1wug]], [[1wum]] – hHAT PCAF + small ligand

Line 80:		Line 68:
	**[[5h86]] - hHAT KAT2A catalytic domain + butyryl CoA<br />		**[[5h86]] - hHAT KAT2A catalytic domain + butyryl CoA<br />
	**[[5trl]] - hHAT KAT2A catalytic domain + succinyl CoA<br />		**[[5trl]] - hHAT KAT2A catalytic domain + succinyl CoA<br />
-	**[[5mlj]] - hHAT KAT2A bromodomain + inhibitor<br />	+	**[[5mlj]], [[6j3p]] - hHAT KAT2A bromodomain + inhibitor<br />
	**[[5lvq]], [[5lvr]], [[5fdz]], [[5fe0]], [[5fe1]], [[5fe2]], [[5fe3]], [[5fe4]], [[5fe5]], [[5fe6]], [[5fe7]], [[5fe8]], [[5fe9]], [[5mkx]] - hHAT KAT2B bromodomain + inhibitor<br />		**[[5lvq]], [[5lvr]], [[5fdz]], [[5fe0]], [[5fe1]], [[5fe2]], [[5fe3]], [[5fe4]], [[5fe5]], [[5fe6]], [[5fe7]], [[5fe8]], [[5fe9]], [[5mkx]] - hHAT KAT2B bromodomain + inhibitor<br />
	**[[4dnc]] – hHAT KAT8 HAT domain + male-specific lethal 1 homolog<br />		**[[4dnc]] – hHAT KAT8 HAT domain + male-specific lethal 1 homolog<br />
Line 86:		Line 74:
	**[[5u2j]] - hHAT KAT6B + H3K14BU peptide<br />		**[[5u2j]] - hHAT KAT6B + H3K14BU peptide<br />
	**[[5gk9]] - hHAT KAT7 + BRD1<br />		**[[5gk9]] - hHAT KAT7 + BRD1<br />
-	**[[5tpx]] - HAT GCN5 + probe – ''Plasmodium falciparum''<br />
	**[[5ml0]] - HAT KAT2B bromodomain + inhibitor - mouse<br />		**[[5ml0]] - HAT KAT2B bromodomain + inhibitor - mouse<br />
		+	**[[1bob]] – yHAT 1 + acetyl-CoA
		+
		+	**[[1qsm]] – yHAT HPA2 + acetyl-CoA
		+
		+	**[[1fy7]], [[1mja]] - yHAT Esa1 + CoA<br />
		+	**[[3to6]] - yHAT Esa1 + H4 peptide<br />
		+	**[[4psw]] - yHAT B + H4 peptide<br />
		+	**[[1e6i]] - yHAT bromodomain + H4 peptide<br />
		+	**[[1mj9]], [[3to9]] - yHAT Esa1 (mutant) + CoA
		+
		+	**[[1mjb]] - yHAT Esa1 (mutant) + acetyl-CoA
		+
		+	**[[3qm0]] - yHAT RTT109 (mutant) + acetyl-CoA
		+
		+	**[[3q35]], [[3q66]], [[3q68]] – yHAT RTT109 + vacuolar protein sorting-associated protein 75
		+
		+	**[[5gcn]] – TtHAT Gcn5 + CoA – ''Tetrahymena thermophila'' - NMR<br />
		+	**[[5tpx]] - HAT GCN5 + probe – ''Plasmodium falciparum''<br />

	*Histone acetyltransferase ternary complexes		*Histone acetyltransferase ternary complexes
Line 94:		Line 99:
	**[[4psx]] - yHAT B + H3 peptide + H4 peptide<br />		**[[4psx]] - yHAT B + H3 peptide + H4 peptide<br />
	**[[5j9q]], [[5j9t]], [[5j9u]], [[5j9w]] - yHAT Esa1 (mutant) + chromatin modification-related protein + enhancer of polycomb-like protein<br />		**[[5j9q]], [[5j9t]], [[5j9u]], [[5j9w]] - yHAT Esa1 (mutant) + chromatin modification-related protein + enhancer of polycomb-like protein<br />
-		+	**[[6cw3]], [[6cw2]] - yHAT GCN5 residues 67-316 + transcriptional adaptor + antibody<br />
	**[[1q2c]] - TtHAT Gcn5 + CoA + histone H4 peptide		**[[1q2c]] - TtHAT Gcn5 + CoA + histone H4 peptide

Line 104:		Line 109:
	**[[3io2]] – hHAT P300 TAZ2 domain <br />		**[[3io2]] – hHAT P300 TAZ2 domain <br />
	**[[4bhw]] - hHAT P300 core (mutant)<br />		**[[4bhw]] - hHAT P300 core (mutant)<br />
		+	**[[6k4n]] - hHAT P300 bromodomain+acetyltransferase domains – Cryo EM<br />
	**[[2mh0]] - hHAT P300 TAZ2 + transcription factor ITF-1<br />		**[[2mh0]] - hHAT P300 TAZ2 + transcription factor ITF-1<br />
	**[[2mh0]], [[2k8f]] - hHAT P300 TAZ2 (mutant) + p53 peptide<br />		**[[2mh0]], [[2k8f]] - hHAT P300 TAZ2 (mutant) + p53 peptide<br />
-	**[[4pzr]], [[4pzs]] - hHAT P300 acetyltransferase domain ~~residues 1287-1664~~ (mutant) + acetyl CoA<br />	+	**[[4pzr]], [[4pzs]] - hHAT P300 acetyltransferase domain (mutant) + acetyl CoA<br />
	**[[4pzt]] - hHAT P300 acetyltransferase domain (mutant) + acetonyl CoA<br />		**[[4pzt]] - hHAT P300 acetyltransferase domain (mutant) + acetonyl CoA<br />
	**[[5lkt]] - hHAT P300 residues 1581-1666 + butyryl CoA<br />		**[[5lkt]] - hHAT P300 residues 1581-1666 + butyryl CoA<br />
Line 112:		Line 118:
	**[[5lkx]] - hHAT P300 core (mutant) + propionyl CoA<br />		**[[5lkx]] - hHAT P300 core (mutant) + propionyl CoA<br />
	**[[5lkz]] - hHAT P300 core (mutant) + crotonyl CoA<br />		**[[5lkz]] - hHAT P300 core (mutant) + crotonyl CoA<br />
-	**[[3biy]] – hHAT P300 acetyltransferase domain ~~residues 1287~~-~~1666~~ + lysine CoA derivative<br />	+	**[[3biy]] – hHAT P300 acetyltransferase domain + lysine CoA derivative<br />
		+	**[[5kj2]] - hHAT P300 acetyltransferase domain + inhibitor<br />
		+	**[[6gyr]] - hHAT P300 core+acetyltransferase domains + lysine CoA derivative<br />
		+	**[[5xzc]] - hHAT P300 core+acetyltransferase domains + p53<br />
	**[[5bt3]], [[5nu5]], [[5lpk]], [[5lpm]] - hHAT P300 bromodomain + inhibitor<br />		**[[5bt3]], [[5nu5]], [[5lpk]], [[5lpm]] - hHAT P300 bromodomain + inhibitor<br />
-		+	**[[6gyt]] - hHAT P300 bromodomain + histone H4 peptide<br />
-		+
	**[[3p57]] - hHAT P300 TAZ2 domain + myocyte-specific enhancer factor 2A + DNA		**[[3p57]] - hHAT P300 TAZ2 domain + myocyte-specific enhancer factor 2A + DNA
	}}		}}

Alexander Berchansky at 12:46, 16 May 2019

Alexander Berchansky — Thu, 16 May 2019 12:46:04 GMT

←Older revision		Revision as of 12:46, 16 May 2019
Line 10:		Line 10:

	== Structural highlights ==		== Structural highlights ==
-	<scene name='46/467281/Cv/5'>HAT binds acetyl CoA</scene> in a <scene name='46/467281/Cv/6'>cleft toward the center of the concave surface</scene> of the protein<ref>PMID:9727486</ref>. Water molecules shown as red spheres.	+	<scene name='46/467281/Cv/7'>HAT binds acetyl CoA</scene> in a <scene name='46/467281/Cv/9'>cleft toward the center of the concave surface</scene> of the protein<ref>PMID:9727486</ref>. Water molecules shown as red spheres.
	</StructureSection>		</StructureSection>
	== 3D Structures of histone acetyltransferase ==		== 3D Structures of histone acetyltransferase ==

Michal Harel at 08:53, 19 June 2018

Michal Harel — Tue, 19 Jun 2018 08:53:40 GMT

←Older revision		Revision as of 08:53, 19 June 2018
Line 17:		Line 17:
	{{#tree:id=OrganizedByTopic\|openlevels=0\|		{{#tree:id=OrganizedByTopic\|openlevels=0\|

-	*Histone acetyltransferase	+	*Histone acetyltransferase; Human domains – catalytic domain residues 497-662; bromodomain residues 729-837;

	**[[1qso]] - yHAT HPA2 – yeast<br />		**[[1qso]] - yHAT HPA2 – yeast<br />
Line 33:		Line 33:
	**[[3gg3]] - hHAT PCAF bromodomain		**[[3gg3]] - hHAT PCAF bromodomain

-	**[[3i3j]] – hHAT P300 bromodomain
-
-	**[[3io2]] – hHAT P300 TAZ2 domain<br />
-	**[[3biy]] – hHAT P300 AT domain<br />
-	**[[4bhw]] - hHAT P300 core (mutant)<br />
	**[[2ou2]] - hHAT HTATIP<br />		**[[2ou2]] - hHAT HTATIP<br />
	**[[2eko]] – hHAT HTATIP histone tail-binding domain - NMR		**[[2eko]] – hHAT HTATIP histone tail-binding domain - NMR

-	**[[1z4r]] – hHAT ~~residues 497-662~~<br />	+	**[[1z4r]] – hHAT catalytic domain<br />
	**[[3toa]] - hHAT Myst1 residues 177-447<br />		**[[3toa]] - hHAT Myst1 residues 177-447<br />
	**[[3tob]] - hHAT Myst1 residues 177-447 (mutant)<br />		**[[3tob]] - hHAT Myst1 residues 177-447 (mutant)<br />
-	**[[2rc4]] – hHAT Myst3 AT domain<br />	+	**[[2rc4]] – hHAT Myst3 acetyltransferase domain<br />
		+	**[[5trm]] - hHAT KAT2A catalytic domain <br />
	**[[4nsq]] - hHAT KAT2B<br />		**[[4nsq]] - hHAT KAT2B<br />
	**[[4qqg]] - hHAT KAT5 N terminal<br />		**[[4qqg]] - hHAT KAT5 N terminal<br />
	**[[2ln0]] - hHAT KAT6A<br />		**[[2ln0]] - hHAT KAT6A<br />
	**[[4ljn]] - hHAT KAT6A double PHD finger<br />		**[[4ljn]] - hHAT KAT6A double PHD finger<br />
		+	**[[5wci]] - hHAT KAT8 residues 174-449 <br />
	**[[5j8c]], [[5j8f]] - hHAT KAT8 residues 177-447 (mutant)<br />		**[[5j8c]], [[5j8f]] - hHAT KAT8 residues 177-447 (mutant)<br />
	**[[2qec]] – HAT HPA2 (mutant) – ''Corynebacterium glutamicum''		**[[2qec]] – HAT HPA2 (mutant) – ''Corynebacterium glutamicum''
Line 71:		Line 68:

	**[[5gcn]] – TtHAT Gcn5 + CoA – ''Tetrahymena thermophila'' - NMR<br />		**[[5gcn]] – TtHAT Gcn5 + CoA – ''Tetrahymena thermophila'' - NMR<br />
-	**[[2mh0]] - hHAT P300 zinc finger + transcription factor ITF-1<br />
-	**[[2mh0]], [[2k8f]] - hHAT P300 zinc finger (mutant) + p53 peptide<br />
-	**[[4pzr]], [[4pzs]] - hHAT P300 acetyltransferase domain (mutant) + acetyl CoA<br />
-	**[[4pzt]] - hHAT P300 acetyltransferase domain (mutant) + acetonyl CoA<br />
-	**[[5lkt]] - hHAT P300 residues 1581-1666 + butyryl CoA<br />
-	**[[5lku]] - hHAT P300 catalytic core + CoA<br />
-	**[[5lkx]] - hHAT P300 catalytic core (mutant) + propionyl CoA<br />
-	**[[5lkz]] - hHAT P300 catalytic core (mutant) + crotonyl CoA<br />
-	**[[5bt3]] - hHAT P300 bromodomain + inhibitor<br />
	**[[1wug]], [[1wum]] – hHAT PCAF + small ligand		**[[1wug]], [[1wum]] – hHAT PCAF + small ligand

Line 89:		Line 77:

	**[[2rnw]], [[2rnx]] - hHAT PCAF bromodomain + histone H3 peptide - NMR<br />		**[[2rnw]], [[2rnx]] - hHAT PCAF bromodomain + histone H3 peptide - NMR<br />
-	**[[5h84]] - hHAT KAT2A + propionyl CoA<br />	+	**[[5h84]] - hHAT KAT2A catalytic domain + propionyl CoA<br />
-	**[[5h86]] - hHAT KAT2A + butyryl CoA<br />	+	**[[5h86]] - hHAT KAT2A catalytic domain + butyryl CoA<br />
-	**[[5lvq]], [[5lvr]], [[5fdz]], [[5fe0]], [[5fe1]], [[5fe2]], [[5fe3]], [[5fe4]], [[5fe5]], [[5fe6]], [[5fe7]], [[5fe8]], [[5fe9]] - hHAT KAT2B bromodomain + inhibitor<br />	+	**[[5trl]] - hHAT KAT2A catalytic domain + succinyl CoA<br />
		+	**[[5mlj]] - hHAT KAT2A bromodomain + inhibitor<br />
		+	**[[5lvq]], [[5lvr]], [[5fdz]], [[5fe0]], [[5fe1]], [[5fe2]], [[5fe3]], [[5fe4]], [[5fe5]], [[5fe6]], [[5fe7]], [[5fe8]], [[5fe9]], [[5mkx]] - hHAT KAT2B bromodomain + inhibitor<br />
	**[[4dnc]] – hHAT KAT8 HAT domain + male-specific lethal 1 homolog<br />		**[[4dnc]] – hHAT KAT8 HAT domain + male-specific lethal 1 homolog<br />
-	**[[3v43]], [[4lk9]], [[4lka]]. [[4llb]], [[5b75]], [[5b76]], [[5b77]], [[5b78]] - hHAT KAT6A + H3.1 peptide<br />	+	**[[3v43]], [[4lk9]], [[4lka]], [[4llb]], [[5b75]], [[5b76]], [[5b77]], [[5b78]] - hHAT KAT6A + H3.1 peptide<br />
	**[[5u2j]] - hHAT KAT6B + H3K14BU peptide<br />		**[[5u2j]] - hHAT KAT6B + H3K14BU peptide<br />
	**[[5gk9]] - hHAT KAT7 + BRD1<br />		**[[5gk9]] - hHAT KAT7 + BRD1<br />
	**[[5tpx]] - HAT GCN5 + probe – ''Plasmodium falciparum''<br />		**[[5tpx]] - HAT GCN5 + probe – ''Plasmodium falciparum''<br />
		+	**[[5ml0]] - HAT KAT2B bromodomain + inhibitor - mouse<br />

	*Histone acetyltransferase ternary complexes		*Histone acetyltransferase ternary complexes
Line 107:		Line 98:

	**[[1q2d]] - TtHAT Gcn5 + CoA + p53 peptide		**[[1q2d]] - TtHAT Gcn5 + CoA + p53 peptide
		+
		+	* Histone acetyltransferase P300; domains – core domain residues 1043-1519; bromodomain residues 1040-1161; acetyltransferase domain residues 1287-1664; TAZ2 domain 1723-1836:
		+
		+	**[[3i3j]] – hHAT P300 bromodomain <br />
		+	**[[3io2]] – hHAT P300 TAZ2 domain <br />
		+	**[[4bhw]] - hHAT P300 core (mutant)<br />
		+	**[[2mh0]] - hHAT P300 TAZ2 + transcription factor ITF-1<br />
		+	**[[2mh0]], [[2k8f]] - hHAT P300 TAZ2 (mutant) + p53 peptide<br />
		+	**[[4pzr]], [[4pzs]] - hHAT P300 acetyltransferase domain residues 1287-1664 (mutant) + acetyl CoA<br />
		+	**[[4pzt]] - hHAT P300 acetyltransferase domain (mutant) + acetonyl CoA<br />
		+	**[[5lkt]] - hHAT P300 residues 1581-1666 + butyryl CoA<br />
		+	**[[5lku]] - hHAT P300 core + CoA<br />
		+	**[[5lkx]] - hHAT P300 core (mutant) + propionyl CoA<br />
		+	**[[5lkz]] - hHAT P300 core (mutant) + crotonyl CoA<br />
		+	**[[3biy]] – hHAT P300 acetyltransferase domain residues 1287-1666 + lysine CoA derivative<br />
		+	**[[5bt3]], [[5nu5]], [[5lpk]], [[5lpm]] - hHAT P300 bromodomain + inhibitor<br />
		+

	**[[3p57]] - hHAT P300 TAZ2 domain + myocyte-specific enhancer factor 2A + DNA		**[[3p57]] - hHAT P300 TAZ2 domain + myocyte-specific enhancer factor 2A + DNA

Michal Harel at 10:35, 12 June 2017

Michal Harel — Mon, 12 Jun 2017 10:35:43 GMT

←Older revision		Revision as of 10:35, 12 June 2017
Line 49:		Line 49:
	**[[2ln0]] - hHAT KAT6A<br />		**[[2ln0]] - hHAT KAT6A<br />
	**[[4ljn]] - hHAT KAT6A double PHD finger<br />		**[[4ljn]] - hHAT KAT6A double PHD finger<br />
		+	**[[5j8c]], [[5j8f]] - hHAT KAT8 residues 177-447 (mutant)<br />
	**[[2qec]] – HAT HPA2 (mutant) – ''Corynebacterium glutamicum''		**[[2qec]] – HAT HPA2 (mutant) – ''Corynebacterium glutamicum''

Line 74:		Line 75:
	**[[4pzr]], [[4pzs]] - hHAT P300 acetyltransferase domain (mutant) + acetyl CoA<br />		**[[4pzr]], [[4pzs]] - hHAT P300 acetyltransferase domain (mutant) + acetyl CoA<br />
	**[[4pzt]] - hHAT P300 acetyltransferase domain (mutant) + acetonyl CoA<br />		**[[4pzt]] - hHAT P300 acetyltransferase domain (mutant) + acetonyl CoA<br />
-		+	**[[5lkt]] - hHAT P300 residues 1581-1666 + butyryl CoA<br />
		+	**[[5lku]] - hHAT P300 catalytic core + CoA<br />
		+	**[[5lkx]] - hHAT P300 catalytic core (mutant) + propionyl CoA<br />
		+	**[[5lkz]] - hHAT P300 catalytic core (mutant) + crotonyl CoA<br />
		+	**[[5bt3]] - hHAT P300 bromodomain + inhibitor<br />
	**[[1wug]], [[1wum]] – hHAT PCAF + small ligand		**[[1wug]], [[1wum]] – hHAT PCAF + small ligand

Line 84:		Line 89:

	**[[2rnw]], [[2rnx]] - hHAT PCAF bromodomain + histone H3 peptide - NMR<br />		**[[2rnw]], [[2rnx]] - hHAT PCAF bromodomain + histone H3 peptide - NMR<br />
		+	**[[5h84]] - hHAT KAT2A + propionyl CoA<br />
		+	**[[5h86]] - hHAT KAT2A + butyryl CoA<br />
		+	**[[5lvq]], [[5lvr]], [[5fdz]], [[5fe0]], [[5fe1]], [[5fe2]], [[5fe3]], [[5fe4]], [[5fe5]], [[5fe6]], [[5fe7]], [[5fe8]], [[5fe9]] - hHAT KAT2B bromodomain + inhibitor<br />
	**[[4dnc]] – hHAT KAT8 HAT domain + male-specific lethal 1 homolog<br />		**[[4dnc]] – hHAT KAT8 HAT domain + male-specific lethal 1 homolog<br />
-	**[[3v43]], [[4lk9]], [[4lka]]. [[4llb]] - hHAT KAT6A + H3.1 peptide<br />	+	**[[3v43]], [[4lk9]], [[4lka]]. [[4llb]], [[5b75]], [[5b76]], [[5b77]], [[5b78]] - hHAT KAT6A + H3.1 peptide<br />
		+	**[[5u2j]] - hHAT KAT6B + H3K14BU peptide<br />
		+	**[[5gk9]] - hHAT KAT7 + BRD1<br />
		+	**[[5tpx]] - HAT GCN5 + probe – ''Plasmodium falciparum''<br />

	*Histone acetyltransferase ternary complexes		*Histone acetyltransferase ternary complexes

-	**[[3q33]] – yHAT RTT109 + vacuolar protein sorting-associated protein 75 + histone H3 peptide	+	**[[3q33]] – yHAT RTT109 + vacuolar protein sorting-associated protein 75 + histone H3 peptide<br />
		+	**[[4psx]] - yHAT B + H3 peptide + H4 peptide<br />
		+	**[[5j9q]], [[5j9t]], [[5j9u]], [[5j9w]] - yHAT Esa1 (mutant) + chromatin modification-related protein + enhancer of polycomb-like protein<br />

	**[[1q2c]] - TtHAT Gcn5 + CoA + histone H4 peptide		**[[1q2c]] - TtHAT Gcn5 + CoA + histone H4 peptide

Alexander Berchansky at 09:44, 30 March 2016

Alexander Berchansky — Wed, 30 Mar 2016 09:44:06 GMT

←Older revision		Revision as of 09:44, 30 March 2016
Line 10:		Line 10:

	== Structural highlights ==		== Structural highlights ==
-	HAT binds acetyl CoA in a cleft toward the center of the concave surface of the protein<ref>PMID:9727486</ref>.	+	<scene name='46/467281/Cv/5'>HAT binds acetyl CoA</scene> in a <scene name='46/467281/Cv/6'>cleft toward the center of the concave surface</scene> of the protein<ref>PMID:9727486</ref>. Water molecules shown as red spheres.
	</StructureSection>		</StructureSection>
	== 3D Structures of histone acetyltransferase ==		== 3D Structures of histone acetyltransferase ==

Alexander Berchansky at 09:16, 30 March 2016

Alexander Berchansky — Wed, 30 Mar 2016 09:16:43 GMT

←Older revision		Revision as of 09:16, 30 March 2016
Line 1:		Line 1:
-	<StructureSection load='1bob' size='350' side='right' caption='Yeast histone acetyltransferase complex with acetyl CoA and Ca+2 ion (green) (PDB entry [[1bob]])' scene=''>	+	<StructureSection load='1bob' size='350' side='right' caption='Yeast histone acetyltransferase complex with acetyl CoA and Ca+2 ion (green) (PDB entry [[1bob]])' scene='46/467281/Cv/1'>
	== Function ==		== Function ==
	'''Histone acetyltransferase''' (HAT) catalyzes the acetylation of lysine residues on histone proteins. The acetyl group is transferred from acetyl-CoA to form ε-N-acetyl lysine. HAT contains a bromodomain – a ca. 110 amino acids domain which binds acetylated lysine. Histone acetylation is linked to transcription activation<ref>PMID:11395403</ref>.		'''Histone acetyltransferase''' (HAT) catalyzes the acetylation of lysine residues on histone proteins. The acetyl group is transferred from acetyl-CoA to form ε-N-acetyl lysine. HAT contains a bromodomain – a ca. 110 amino acids domain which binds acetylated lysine. Histone acetylation is linked to transcription activation<ref>PMID:11395403</ref>.