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1aoi
From Proteopedia
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| - | [[Image:1aoi.png|left|200px]] | ||
| - | + | ==COMPLEX BETWEEN NUCLEOSOME CORE PARTICLE (H3,H4,H2A,H2B) AND 146 BP LONG DNA FRAGMENT== | |
| - | + | <StructureSection load='1aoi' size='340' side='right'caption='[[1aoi]], [[Resolution|resolution]] 2.80Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[1aoi]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. The July 2000 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Nucleosome'' by David S. Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2000_7 10.2210/rcsb_pdb/mom_2000_7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AOI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AOI 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]] 2.8Å</td></tr> | |
| - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</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=1aoi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aoi OCA], [https://pdbe.org/1aoi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1aoi RCSB], [https://www.ebi.ac.uk/pdbsum/1aoi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1aoi ProSAT]</span></td></tr> |
| - | [[1aoi]] is a 10 chain structure | + | </table> |
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/H2B11_XENLA H2B11_XENLA] Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ao/1aoi_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1aoi ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
==See Also== | ==See Also== | ||
| - | *[[Histone|Histone]] | + | *[[Histone 3D structures|Histone 3D structures]] |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
| - | + | [[Category: Large Structures]] | |
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[[Category: Nucleosome]] | [[Category: Nucleosome]] | ||
[[Category: RCSB PDB Molecule of the Month]] | [[Category: RCSB PDB Molecule of the Month]] | ||
[[Category: Xenopus laevis]] | [[Category: Xenopus laevis]] | ||
| - | [[Category: Luger | + | [[Category: Luger K]] |
| - | [[Category: Maeder | + | [[Category: Maeder AW]] |
| - | [[Category: Richmond | + | [[Category: Richmond RK]] |
| - | [[Category: Richmond | + | [[Category: Richmond TJ]] |
| - | [[Category: Sargent | + | [[Category: Sargent DF]] |
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Current revision
COMPLEX BETWEEN NUCLEOSOME CORE PARTICLE (H3,H4,H2A,H2B) AND 146 BP LONG DNA FRAGMENT
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