5gk9: Difference between revisions

Revision as of 13:42, 29 March 2017

Crystal structure of human HBO1 in complex with BRPF2

Structural highlights

5gk9 is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	ACO, ZN
Activity:	Histone acetyltransferase, with EC number 2.3.1.48
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[KAT7_HUMAN] Component of the HBO1 complex which has a histone H4-specific acetyltransferase activity, a reduced activity toward histone H3 and is responsible for the bulk of histone H4 acetylation in vivo. Through chromatin acetylation it may regulate DNA replication and act as a coactivator of TP53-dependent transcription. Acts as a coactivator of the licensing factor CDT1 (PubMed:18832067). Specifically represses AR-mediated transcription.^[1] ^[2] ^[3] ^[4] ^[5]

References

↑ Iizuka M, Stillman B. Histone acetyltransferase HBO1 interacts with the ORC1 subunit of the human initiator protein. J Biol Chem. 1999 Aug 13;274(33):23027-34. PMID:10438470
↑ Sharma M, Zarnegar M, Li X, Lim B, Sun Z. Androgen receptor interacts with a novel MYST protein, HBO1. J Biol Chem. 2000 Nov 10;275(45):35200-8. PMID:10930412 doi:https://dx.doi.org/10.1074/jbc.M004838200
↑ Burke TW, Cook JG, Asano M, Nevins JR. Replication factors MCM2 and ORC1 interact with the histone acetyltransferase HBO1. J Biol Chem. 2001 May 4;276(18):15397-408. Epub 2001 Jan 24. PMID:11278932 doi:https://dx.doi.org/10.1074/jbc.M011556200
↑ Doyon Y, Cayrou C, Ullah M, Landry AJ, Cote V, Selleck W, Lane WS, Tan S, Yang XJ, Cote J. ING tumor suppressor proteins are critical regulators of chromatin acetylation required for genome expression and perpetuation. Mol Cell. 2006 Jan 6;21(1):51-64. PMID:16387653 doi:10.1016/j.molcel.2005.12.007
↑ Miotto B, Struhl K. HBO1 histone acetylase is a coactivator of the replication licensing factor Cdt1. Genes Dev. 2008 Oct 1;22(19):2633-8. doi: 10.1101/gad.1674108. PMID:18832067 doi:https://dx.doi.org/10.1101/gad.1674108

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OCA

[1] Iizuka M, Stillman B. Histone acetyltransferase HBO1 interacts with the ORC1 subunit of the human initiator protein. J Biol Chem. 1999 Aug 13;274(33):23027-34. PMID:10438470

[2] Sharma M, Zarnegar M, Li X, Lim B, Sun Z. Androgen receptor interacts with a novel MYST protein, HBO1. J Biol Chem. 2000 Nov 10;275(45):35200-8. PMID:10930412 doi:https://dx.doi.org/10.1074/jbc.M004838200

[3] Burke TW, Cook JG, Asano M, Nevins JR. Replication factors MCM2 and ORC1 interact with the histone acetyltransferase HBO1. J Biol Chem. 2001 May 4;276(18):15397-408. Epub 2001 Jan 24. PMID:11278932 doi:https://dx.doi.org/10.1074/jbc.M011556200

[4] Doyon Y, Cayrou C, Ullah M, Landry AJ, Cote V, Selleck W, Lane WS, Tan S, Yang XJ, Cote J. ING tumor suppressor proteins are critical regulators of chromatin acetylation required for genome expression and perpetuation. Mol Cell. 2006 Jan 6;21(1):51-64. PMID:16387653 doi:10.1016/j.molcel.2005.12.007

[5] Miotto B, Struhl K. HBO1 histone acetylase is a coactivator of the replication licensing factor Cdt1. Genes Dev. 2008 Oct 1;22(19):2633-8. doi: 10.1101/gad.1674108. PMID:18832067 doi:https://dx.doi.org/10.1101/gad.1674108

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 5gk9 is ON HOLD  until Paper Publication
+==Crystal structure of human HBO1 in complex with BRPF2==
+<StructureSection load='5gk9' size='340' side='right' caption='[[5gk9]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
-Authors: Tao, Y., Zhu, J., Xu, S., Ding, J.
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5gk9]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5GK9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5GK9 FirstGlance]. <br>
-Description: Crystal structure of a new HAT complex
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACO:ACETYL+COENZYME+*A'>ACO</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-[[Category: Unreleased Structures]]
+<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Histone_acetyltransferase Histone acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.48 2.3.1.48] </span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5gk9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5gk9 OCA], [http://pdbe.org/5gk9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5gk9 RCSB], [http://www.ebi.ac.uk/pdbsum/5gk9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5gk9 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[[http://www.uniprot.org/uniprot/KAT7_HUMAN KAT7_HUMAN]] Component of the HBO1 complex which has a histone H4-specific acetyltransferase activity, a reduced activity toward histone H3 and is responsible for the bulk of histone H4 acetylation in vivo. Through chromatin acetylation it may regulate DNA replication and act as a coactivator of TP53-dependent transcription. Acts as a coactivator of the licensing factor CDT1 (PubMed:18832067). Specifically represses AR-mediated transcription.<ref>PMID:10438470</ref> <ref>PMID:10930412</ref> <ref>PMID:11278932</ref> <ref>PMID:16387653</ref> <ref>PMID:18832067</ref>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Histone acetyltransferase]]
 [[Category: Ding, J]]
+[[Category: Tao, Y]]
+[[Category: Xu, S]]
 [[Category: Zhu, J]]
-[[Category: Xu, S]]
+[[Category: Hat]]
-[[Category: Tao, Y]]
+[[Category: Transferase-metal binding protein complex]]

5gk9: Difference between revisions

Revision as of 13:42, 29 March 2017

Crystal structure of human HBO1 in complex with BRPF2

Structural highlights

Function

References

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