5gk9

From Proteopedia

(Difference between revisions)

Revision as of 07:32, 6 December 2017

Crystal structure of human HBO1 in complex with BRPF2

Structural highlights

5gk9 is a 2 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Gene:	KAT7, HBO1, HBOa, MYST2 (HUMAN), BRD1 (HUMAN)
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]

Publication Abstract from PubMed

HBO1, a member of the MYST family of histone acetyltransferases (HATs), is required for global acetylation of histone H3K14 and embryonic development. It functions as a catalytic subunit in multisubunit complexes comprising a BRPF1/2/3 or JADE1/2/3 scaffold protein, and two accessory proteins. BRPF2 has been shown to be important for the HAT activity of HBO1 toward H3K14. Here we demonstrated that BRPF2 can regulate the HAT activity of HBO1 toward free H3 and H4, and nucleosomal H3. Particularly, a short N-terminal region of BRPF2 is sufficient for binding to HBO1 and can potentiate its activity toward H3K14. The crystal structure of the HBO1 MYST domain in complex with this segment of BRPF2 together with the biochemical and cell biological data revealed the key residues responsible for the HBO1-BRPF2 interaction. Our structural and functional data together indicate that the N-terminal region of BRPF2 plays an important role in the binding of HBO1 and a minor role in the binding of nucleosomes, which provide new mechanistic insights into the regulation of the HAT activity of HBO1 by BRPF2.

Structural and mechanistic insights into regulation of HBO1 histone acetyltransferase activity by BRPF2.,Tao Y, Zhong C, Zhu J, Xu S, Ding J Nucleic Acids Res. 2017 Jun 2;45(10):5707-5719. doi: 10.1093/nar/gkx142. PMID:28334966^[6]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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:http://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:http://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:http://dx.doi.org/10.1101/gad.1674108
↑ Tao Y, Zhong C, Zhu J, Xu S, Ding J. Structural and mechanistic insights into regulation of HBO1 histone acetyltransferase activity by BRPF2. Nucleic Acids Res. 2017 Jun 2;45(10):5707-5719. doi: 10.1093/nar/gkx142. PMID:28334966 doi:http://dx.doi.org/10.1093/nar/gkx142

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5gk9"

@@ Line 3: / Line 3: @@
 <StructureSection load='5gk9' size='340' side='right' caption='[[5gk9]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
 == 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>
+<table><tr><td colspan='2'>[[5gk9]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. 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>
 </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>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">KAT7, HBO1, HBOa, MYST2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), BRD1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
 <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>
@@ Line 10: / Line 11: @@
 == 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>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+HBO1, a member of the MYST family of histone acetyltransferases (HATs), is required for global acetylation of histone H3K14 and embryonic development. It functions as a catalytic subunit in multisubunit complexes comprising a BRPF1/2/3 or JADE1/2/3 scaffold protein, and two accessory proteins. BRPF2 has been shown to be important for the HAT activity of HBO1 toward H3K14. Here we demonstrated that BRPF2 can regulate the HAT activity of HBO1 toward free H3 and H4, and nucleosomal H3. Particularly, a short N-terminal region of BRPF2 is sufficient for binding to HBO1 and can potentiate its activity toward H3K14. The crystal structure of the HBO1 MYST domain in complex with this segment of BRPF2 together with the biochemical and cell biological data revealed the key residues responsible for the HBO1-BRPF2 interaction. Our structural and functional data together indicate that the N-terminal region of BRPF2 plays an important role in the binding of HBO1 and a minor role in the binding of nucleosomes, which provide new mechanistic insights into the regulation of the HAT activity of HBO1 by BRPF2.
+Structural and mechanistic insights into regulation of HBO1 histone acetyltransferase activity by BRPF2.,Tao Y, Zhong C, Zhu J, Xu S, Ding J Nucleic Acids Res. 2017 Jun 2;45(10):5707-5719. doi: 10.1093/nar/gkx142. PMID:28334966<ref>PMID:28334966</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 5gk9" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
@@ Line 15: / Line 25: @@
 </StructureSection>
 [[Category: Histone acetyltransferase]]
+[[Category: Human]]
 [[Category: Ding, J]]
 [[Category: Tao, Y]]

5gk9

From Proteopedia

Revision as of 07:32, 6 December 2017

Crystal structure of human HBO1 in complex with BRPF2

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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