4ym5
From Proteopedia
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| - | ''' | + | ==Crystal structure of the human nucleosome containing 6-4PP (inside)== |
| + | <StructureSection load='4ym5' size='340' side='right' caption='[[4ym5]], [[Resolution|resolution]] 4.00Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4ym5]] is a 10 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4YM5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4YM5 FirstGlance]. <br> | ||
| + | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=T64:(6-4)PHOTOPRODUCT'>T64</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ym6|4ym6]]</td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ym5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ym5 OCA], [http://pdbe.org/4ym5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ym5 RCSB], [http://www.ebi.ac.uk/pdbsum/4ym5 PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/H2B1J_HUMAN H2B1J_HUMAN]] 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.<ref>PMID:11859126</ref> <ref>PMID:12860195</ref> <ref>PMID:15019208</ref> Has broad antibacterial activity. May contribute to the formation of the functional antimicrobial barrier of the colonic epithelium, and to the bactericidal activity of amniotic fluid.<ref>PMID:11859126</ref> <ref>PMID:12860195</ref> <ref>PMID:15019208</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | UV-DDB, an initiation factor for the nucleotide excision repair pathway, recognizes 6-4PP lesions through a base flipping mechanism. As genomic DNA is almost entirely accommodated within nucleosomes, the flipping of the 6-4PP bases is supposed to be extremely difficult if the lesion occurs in a nucleosome, especially on the strand directly contacting the histone surface. Here we report that UV-DDB binds efficiently to nucleosomal 6-4PPs that are rotationally positioned on the solvent accessible or occluded surface. We determined the crystal structures of nucleosomes containing 6-4PPs in these rotational positions, and found that the 6-4PP DNA regions were flexibly disordered, especially in the strand exposed to the solvent. This characteristic of 6-4PP may facilitate UV-DDB binding to the damaged nucleosome. We present the first atomic-resolution pictures of the detrimental DNA cross-links of neighboring pyrimidine bases within the nucleosome, and provide the mechanistic framework for lesion recognition by UV-DDB in chromatin. | ||
| - | + | Structural basis of pyrimidine-pyrimidone (6-4) photoproduct recognition by UV-DDB in the nucleosome.,Osakabe A, Tachiwana H, Kagawa W, Horikoshi N, Matsumoto S, Hasegawa M, Matsumoto N, Toga T, Yamamoto J, Hanaoka F, Thoma NH, Sugasawa K, Iwai S, Kurumizaka H Sci Rep. 2015 Nov 17;5:16330. doi: 10.1038/srep16330. PMID:26573481<ref>PMID:26573481</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 4ym5" style="background-color:#fffaf0;"></div> | |
| - | [[Category: | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Hanaoka, F]] | ||
| + | [[Category: Hasegawa, M]] | ||
| + | [[Category: Horikoshi, N]] | ||
| + | [[Category: Iwai, S]] | ||
| + | [[Category: Kagawa, W]] | ||
[[Category: Kurumizaka, H]] | [[Category: Kurumizaka, H]] | ||
| - | [[Category: | + | [[Category: Matsumoto, N]] |
| + | [[Category: Matsumoto, S]] | ||
[[Category: Osakabe, A]] | [[Category: Osakabe, A]] | ||
[[Category: Sugasawa, K]] | [[Category: Sugasawa, K]] | ||
| + | [[Category: Tachiwana, H]] | ||
| + | [[Category: Thoma, N H]] | ||
| + | [[Category: Toga, T]] | ||
[[Category: Yamamoto, J]] | [[Category: Yamamoto, J]] | ||
| - | [[Category: | + | [[Category: Dna binding]] |
| - | [[Category: | + | [[Category: Histone]] |
| - | [[Category: | + | [[Category: Nucleosome]] |
| - | [[Category: | + | [[Category: Structural protein-dna complex]] |
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Revision as of 16:11, 2 December 2015
Crystal structure of the human nucleosome containing 6-4PP (inside)
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