5t5k

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'''Unreleased structure'''
 
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The entry 5t5k is ON HOLD until Paper Publication
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==Structure of histone-based chromatin in Archaea==
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<StructureSection load='5t5k' size='340' side='right'caption='[[5t5k]], [[Resolution|resolution]] 4.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5t5k]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanothermus_fervidus Methanothermus fervidus] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5T5K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5T5K FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 4&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CAC:CACODYLATE+ION'>CAC</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5t5k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5t5k OCA], [https://pdbe.org/5t5k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5t5k RCSB], [https://www.ebi.ac.uk/pdbsum/5t5k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5t5k ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/HMFB_METFE HMFB_METFE] Binds and compact DNA (95 to 150 base pairs) to form nucleosome-like structures that contain positive DNA supercoils. Increases the resistance of DNA to thermal denaturation.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Small basic proteins present in most Archaea share a common ancestor with the eukaryotic core histones. We report the crystal structure of an archaeal histone-DNA complex. DNA wraps around an extended polymer, formed by archaeal histone homodimers, in a quasi-continuous superhelix with the same geometry as DNA in the eukaryotic nucleosome. Substitutions of a conserved glycine at the interface of adjacent protein layers destabilize archaeal chromatin, reduce growth rate, and impair transcription regulation, confirming the biological importance of the polymeric structure. Our data establish that the histone-based mechanism of DNA compaction predates the nucleosome, illuminating the origin of the nucleosome.
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Authors:
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Structure of histone-based chromatin in Archaea.,Mattiroli F, Bhattacharyya S, Dyer PN, White AE, Sandman K, Burkhart BW, Byrne KR, Lee T, Ahn NG, Santangelo TJ, Reeve JN, Luger K Science. 2017 Aug 11;357(6351):609-612. doi: 10.1126/science.aaj1849. PMID:28798133<ref>PMID:28798133</ref>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 5t5k" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Methanothermus fervidus]]
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[[Category: Synthetic construct]]
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[[Category: Bhattacharyya S]]
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[[Category: Dyer PN]]
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[[Category: Luger K]]
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[[Category: Mattiroli F]]
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[[Category: Reeve JN]]
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[[Category: Sandman K]]

Current revision

Structure of histone-based chromatin in Archaea

PDB ID 5t5k

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