Histone acetyltransferase

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== 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 ==
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{{#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
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**[[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
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**[[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 />
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**[[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
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**[[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
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**[[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 />
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**[[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
}}
}}

Revision as of 08:23, 28 July 2019

Yeast histone acetyltransferase complex with acetyl CoA and Ca+2 ion (green) (PDB entry 1bob)

Drag the structure with the mouse to rotate

3D Structures of histone acetyltransferase

Updated on 28-July-2019

References

  1. ↑ Roth SY, Denu JM, Allis CD. Histone acetyltransferases. Annu Rev Biochem. 2001;70:81-120. PMID:11395403 doi:10.1146/annurev.biochem.70.1.81
  2. ↑ Dekker FJ, van den Bosch T, Martin NI. Small molecule inhibitors of histone acetyltransferases and deacetylases are potential drugs for inflammatory diseases. Drug Discov Today. 2014 May;19(5):654-60. doi: 10.1016/j.drudis.2013.11.012. Epub, 2013 Nov 21. PMID:24269836 doi:http://dx.doi.org/10.1016/j.drudis.2013.11.012
  3. ↑ Van Beekum O, Kalkhoven E. Aberrant forms of histone acetyltransferases in human disease. Subcell Biochem. 2007;41:233-62. PMID:17484131
  4. ↑ Dutnall RN, Tafrov ST, Sternglanz R, Ramakrishnan V. Structure of the histone acetyltransferase Hat1: a paradigm for the GCN5-related N-acetyltransferase superfamily. Cell. 1998 Aug 21;94(4):427-38. PMID:9727486

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky

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