Histone acetyltransferase

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{{#tree:id=OrganizedByTopic|openlevels=0|
{{#tree:id=OrganizedByTopic|openlevels=0|
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*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

Revision as of 08:53, 19 June 2018

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

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3D Structures of histone acetyltransferase

Updated on 19-June-2018


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

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Michal Harel, Alexander Berchansky

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