6jq0

From Proteopedia

(Difference between revisions)

Current revision

CryoEM structure of Abo1 Walker B (E372Q) mutant hexamer - ATP complex

6jq0, resolution 3.54Å

Structural highlights

6jq0 is a 7 chain structure with sequence from Schizosaccharomyces pombe 972h- and Spodoptera frugiperda. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Electron Microscopy, Resolution 3.54Å
Ligands:
Experimental data:	Check to display Experimental Data
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ATD2_SCHPO ATPase histone chaperone which facilitates loading of histone H3-H4 onto DNA in an ATP-dependent manner (PubMed:31848341, PubMed:33658433). Plays a genome-wide role in nucleosome organization and establishment of chromatin (PubMed:26582768, PubMed:31848341). Also plays a role in heterochromatin assembly by stabilizing recruitment of the histone methyltransferase clr4 to methylated histone H3, to promote the transition from H3K9me2 to H3K9me3 (PubMed:32269268).^[1] ^[2] ^[3] ^[4]

Publication Abstract from PubMed

The fundamental unit of chromatin, the nucleosome, is an intricate structure that requires histone chaperones for assembly. ATAD2 AAA+ ATPases are a family of histone chaperones that regulate nucleosome density and chromatin dynamics. Here, we demonstrate that the fission yeast ATAD2 homolog, Abo1, deposits histone H3-H4 onto DNA in an ATP-hydrolysis-dependent manner by in vitro reconstitution and single-tethered DNA curtain assays. We present cryo-EM structures of an ATAD2 family ATPase to atomic resolution in three different nucleotide states, revealing unique structural features required for histone loading on DNA, and directly visualize the transitions of Abo1 from an asymmetric spiral (ATP-state) to a symmetric ring (ADP- and apo-states) using high-speed atomic force microscopy (HS-AFM). Furthermore, we find that the acidic pore of ATP-Abo1 binds a peptide substrate which is suggestive of a histone tail. Based on these results, we propose a model whereby Abo1 facilitates H3-H4 loading by utilizing ATP.

Structural basis of nucleosome assembly by the Abo1 AAA+ ATPase histone chaperone.,Cho C, Jang J, Kang Y, Watanabe H, Uchihashi T, Kim SJ, Kato K, Lee JY, Song JJ Nat Commun. 2019 Dec 17;10(1):5764. doi: 10.1038/s41467-019-13743-9. PMID:31848341^[5]

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

References

↑ Gal C, Murton HE, Subramanian L, Whale AJ, Moore KM, Paszkiewicz K, Codlin S, Bähler J, Creamer KM, Partridge JF, Allshire RC, Kent NA, Whitehall SK. Abo1, a conserved bromodomain AAA-ATPase, maintains global nucleosome occupancy and organisation. EMBO Rep. 2016 Jan;17(1):79-93. PMID:26582768 doi:10.15252/embr.201540476
↑ Cho C, Jang J, Kang Y, Watanabe H, Uchihashi T, Kim SJ, Kato K, Lee JY, Song JJ. Structural basis of nucleosome assembly by the Abo1 AAA+ ATPase histone chaperone. Nat Commun. 2019 Dec 17;10(1):5764. doi: 10.1038/s41467-019-13743-9. PMID:31848341 doi:http://dx.doi.org/10.1038/s41467-019-13743-9
↑ Dong W, Oya E, Zahedi Y, Prasad P, Svensson JP, Lennartsson A, Ekwall K, Durand-Dubief M. Abo1 is required for the H3K9me2 to H3K9me3 transition in heterochromatin. Sci Rep. 2020 Apr 8;10(1):6055. PMID:32269268 doi:10.1038/s41598-020-63209-y
↑ Kang Y, Cho C, Lee KS, Song JJ, Lee JY. Single-Molecule Imaging Reveals the Mechanism Underlying Histone Loading of Schizosaccharomyces pombe AAA+ ATPase Abo1. Mol Cells. 2021 Feb 28;44(2):79-87. PMID:33658433 doi:10.14348/molcells.2021.2242
↑ Cho C, Jang J, Kang Y, Watanabe H, Uchihashi T, Kim SJ, Kato K, Lee JY, Song JJ. Structural basis of nucleosome assembly by the Abo1 AAA+ ATPase histone chaperone. Nat Commun. 2019 Dec 17;10(1):5764. doi: 10.1038/s41467-019-13743-9. PMID:31848341 doi:http://dx.doi.org/10.1038/s41467-019-13743-9

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/6jq0"

@@ Line 3: / Line 3: @@
 <SX load='6jq0' size='340' side='right' viewer='molstar' caption='[[6jq0]], [[Resolution|resolution]] 3.54&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[6jq0]] is a 7 chain structure with sequence from [http://en.wikipedia.org/wiki/Fission_yeast Fission yeast] and [http://en.wikipedia.org/wiki/Spodoptera_frugiperda Spodoptera frugiperda]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6JQ0 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6JQ0 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[6jq0]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Schizosaccharomyces_pombe_972h- Schizosaccharomyces pombe 972h-] and [https://en.wikipedia.org/wiki/Spodoptera_frugiperda Spodoptera frugiperda]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6JQ0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6JQ0 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.54&#8491;</td></tr>
-<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</scene></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene></td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6jpq|6jpq]], [[6jpu|6jpu]]</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=6jq0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6jq0 OCA], [https://pdbe.org/6jq0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6jq0 RCSB], [https://www.ebi.ac.uk/pdbsum/6jq0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6jq0 ProSAT]</span></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SPAC31G5.19 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=284812 Fission yeast])</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6jq0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6jq0 OCA], [http://pdbe.org/6jq0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6jq0 RCSB], [http://www.ebi.ac.uk/pdbsum/6jq0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6jq0 ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/ATD2_SCHPO ATD2_SCHPO] ATPase histone chaperone which facilitates loading of histone H3-H4 onto DNA in an ATP-dependent manner (PubMed:31848341, PubMed:33658433). Plays a genome-wide role in nucleosome organization and establishment of chromatin (PubMed:26582768, PubMed:31848341). Also plays a role in heterochromatin assembly by stabilizing recruitment of the histone methyltransferase clr4 to methylated histone H3, to promote the transition from H3K9me2 to H3K9me3 (PubMed:32269268).<ref>PMID:26582768</ref> <ref>PMID:31848341</ref> <ref>PMID:32269268</ref> <ref>PMID:33658433</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 23: / Line 23: @@
 __TOC__
 </SX>
-[[Category: Fission yeast]]
 [[Category: Large Structures]]
+[[Category: Schizosaccharomyces pombe 972h-]]
 [[Category: Spodoptera frugiperda]]
-[[Category: Cho, C]]
+[[Category: Cho C]]
-[[Category: Jang, J]]
+[[Category: Jang J]]
-[[Category: Song, J J]]
+[[Category: Song JJ]]
-[[Category: Aaa+ atpase histone chaperone]]
-[[Category: Chaperone]]

6jq0

From Proteopedia

Current revision

CryoEM structure of Abo1 Walker B (E372Q) mutant hexamer - ATP complex

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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