5bo0
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5bo0]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5BO0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5BO0 FirstGlance]. <br> | <table><tr><td colspan='2'>[[5bo0]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5BO0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5BO0 FirstGlance]. <br> | ||
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.906Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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=5bo0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5bo0 OCA], [https://pdbe.org/5bo0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5bo0 RCSB], [https://www.ebi.ac.uk/pdbsum/5bo0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5bo0 ProSAT]</span></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=5bo0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5bo0 OCA], [https://pdbe.org/5bo0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5bo0 RCSB], [https://www.ebi.ac.uk/pdbsum/5bo0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5bo0 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/H32_HUMAN H32_HUMAN] | [https://www.uniprot.org/uniprot/H32_HUMAN H32_HUMAN] | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | During DNA replication, chromatin is reassembled by recycling of modified old histones and deposition of new ones. How histone dynamics integrates with DNA replication to maintain genome and epigenome information remains unclear. Here, we reveal how human MCM2, part of the replicative helicase, chaperones histones H3-H4. Our first structure shows an H3-H4 tetramer bound by two MCM2 histone-binding domains (HBDs), which hijack interaction sites used by nucleosomal DNA. Our second structure reveals MCM2 and ASF1 cochaperoning an H3-H4 dimer. Mutational analyses show that the MCM2 HBD is required for MCM2-7 histone-chaperone function and normal cell proliferation. Further, we show that MCM2 can chaperone both new and old canonical histones H3-H4 as well as H3.3 and CENPA variants. The unique histone-binding mode of MCM2 thus endows the replicative helicase with ideal properties for recycling histones genome wide during DNA replication. | ||
| - | |||
| - | A unique binding mode enables MCM2 to chaperone histones H3-H4 at replication forks.,Huang H, Stromme CB, Saredi G, Hodl M, Strandsby A, Gonzalez-Aguilera C, Chen S, Groth A, Patel DJ Nat Struct Mol Biol. 2015 Jul 13. doi: 10.1038/nsmb.3055. PMID:26167883<ref>PMID:26167883</ref> | ||
| - | |||
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 5bo0" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Anti-silencing factor 3D structures|Anti-silencing factor 3D structures]] | *[[Anti-silencing factor 3D structures|Anti-silencing factor 3D structures]] | ||
*[[Histone 3D structures|Histone 3D structures]] | *[[Histone 3D structures|Histone 3D structures]] | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Current revision
Crystal structure of Human MCM2 HBD and ASF1b chaperoning a histone H3.2-H4 dimer
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