7xay

From Proteopedia

(Difference between revisions)

Current revision

Crystal structure of Hat1-Hat2-Asf1-H3-H4

Structural highlights

7xay is a 5 chain structure with sequence from Aspergillus fumigatus Af293 and Saccharomyces cerevisiae S288C. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 3.3Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

C562_ECOLX Electron-transport protein of unknown function.HAT1_YEAST Catalytic component of the histone acetylase B (HAT-B) complex. Acetylates 'Lys-12' of free histone H4 in the cytoplasm. The complex is also found in the nucleus, however it is not certain that it modifies histone H4 when packaged in chromatin. Histone H4 'Lys-12' acetylation is required for telomeric silencing. Has intrinsic substrate specificity that modifies lysine in recognition sequence GXGKXG. Involved in DNA double-strand break repair.^[1] ^[2] ^[3] ^[4] ^[5]

Publication Abstract from PubMed

Chaperones influence histone conformation and intermolecular interaction in multiprotein complexes, and the structures obtained with full-length histones often provide more accurate and comprehensive views. Here, our structure of the Hat1-Hat2 acetyltransferase complex bound to Asf1-H3-H4 shows that the core domains of H3 and H4 are involved in binding Hat1 and Hat2, and the N-terminal tail of H3 makes extensive interaction with Hat2. These findings expand the knowledge about histone-protein interaction and implicate a function of Hat2/RbAp46/48, which is a versatile histone chaperone found in many chromatin-associated complexes, in the passing of histones between chaperones.

Topography of histone H3-H4 interaction with the Hat1-Hat2 acetyltransferase complex.,Yue Y, Yang WS, Zhang L, Liu CP, Xu RM Genes Dev. 2022 Apr 1;36(7-8):408-413. doi: 10.1101/gad.349099.121. Epub 2022 Apr , 7. PMID:35393344^[6]

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

References

↑ Kleff S, Andrulis ED, Anderson CW, Sternglanz R. Identification of a gene encoding a yeast histone H4 acetyltransferase. J Biol Chem. 1995 Oct 20;270(42):24674-7. PMID:7559580
↑ Kelly TJ, Qin S, Gottschling DE, Parthun MR. Type B histone acetyltransferase Hat1p participates in telomeric silencing. Mol Cell Biol. 2000 Oct;20(19):7051-8. PMID:10982821
↑ Qin S, Parthun MR. Histone H3 and the histone acetyltransferase Hat1p contribute to DNA double-strand break repair. Mol Cell Biol. 2002 Dec;22(23):8353-65. PMID:12417736
↑ Poveda A, Pamblanco M, Tafrov S, Tordera V, Sternglanz R, Sendra R. Hif1 is a component of yeast histone acetyltransferase B, a complex mainly localized in the nucleus. J Biol Chem. 2004 Apr 16;279(16):16033-43. Epub 2004 Feb 3. PMID:14761951 doi:http://dx.doi.org/10.1074/jbc.M314228200
↑ Ai X, Parthun MR. The nuclear Hat1p/Hat2p complex: a molecular link between type B histone acetyltransferases and chromatin assembly. Mol Cell. 2004 Apr 23;14(2):195-205. PMID:15099519
↑ Yue Y, Yang WS, Zhang L, Liu CP, Xu RM. Topography of histone H3-H4 interaction with the Hat1-Hat2 acetyltransferase complex. Genes Dev. 2022 Apr 1;36(7-8):408-413. PMID:35393344 doi:10.1101/gad.349099.121

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/7xay"

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 7xay is ON HOLD
+==Crystal structure of Hat1-Hat2-Asf1-H3-H4==
+<StructureSection load='7xay' size='340' side='right'caption='[[7xay]], [[Resolution|resolution]] 3.30&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[7xay]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Aspergillus_fumigatus_Af293 Aspergillus fumigatus Af293] and [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7XAY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7XAY FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.3&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=COA:COENZYME+A'>COA</scene></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7xay FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7xay OCA], [https://pdbe.org/7xay PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7xay RCSB], [https://www.ebi.ac.uk/pdbsum/7xay PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7xay ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/C562_ECOLX C562_ECOLX] Electron-transport protein of unknown function.[https://www.uniprot.org/uniprot/HAT1_YEAST HAT1_YEAST] Catalytic component of the histone acetylase B (HAT-B) complex. Acetylates 'Lys-12' of free histone H4 in the cytoplasm. The complex is also found in the nucleus, however it is not certain that it modifies histone H4 when packaged in chromatin. Histone H4 'Lys-12' acetylation is required for telomeric silencing. Has intrinsic substrate specificity that modifies lysine in recognition sequence GXGKXG. Involved in DNA double-strand break repair.<ref>PMID:7559580</ref> <ref>PMID:10982821</ref> <ref>PMID:12417736</ref> <ref>PMID:14761951</ref> <ref>PMID:15099519</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Chaperones influence histone conformation and intermolecular interaction in multiprotein complexes, and the structures obtained with full-length histones often provide more accurate and comprehensive views. Here, our structure of the Hat1-Hat2 acetyltransferase complex bound to Asf1-H3-H4 shows that the core domains of H3 and H4 are involved in binding Hat1 and Hat2, and the N-terminal tail of H3 makes extensive interaction with Hat2. These findings expand the knowledge about histone-protein interaction and implicate a function of Hat2/RbAp46/48, which is a versatile histone chaperone found in many chromatin-associated complexes, in the passing of histones between chaperones.
-Authors:
+Topography of histone H3-H4 interaction with the Hat1-Hat2 acetyltransferase complex.,Yue Y, Yang WS, Zhang L, Liu CP, Xu RM Genes Dev. 2022 Apr 1;36(7-8):408-413. doi: 10.1101/gad.349099.121. Epub 2022 Apr , 7. PMID:35393344<ref>PMID:35393344</ref>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 7xay" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Anti-silencing factor 3D structures|Anti-silencing factor 3D structures]]
+*[[Histone 3D structures|Histone 3D structures]]
+*[[Histone acetyltransferase 3D structures|Histone acetyltransferase 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Aspergillus fumigatus Af293]]
+[[Category: Large Structures]]
+[[Category: Saccharomyces cerevisiae S288C]]
+[[Category: Xu RM]]
+[[Category: Yang WS]]
+[[Category: Yue Y]]

7xay

From Proteopedia

Current revision

Crystal structure of Hat1-Hat2-Asf1-H3-H4

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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