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4xyi
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Mis16 with H4 peptide== | |
| + | <StructureSection load='4xyi' size='340' side='right'caption='[[4xyi]], [[Resolution|resolution]] 3.00Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4xyi]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Schizosaccharomyces_japonicus_yFS275 Schizosaccharomyces japonicus yFS275]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XYI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4XYI 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]] 3Å</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=4xyi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xyi OCA], [https://pdbe.org/4xyi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4xyi RCSB], [https://www.ebi.ac.uk/pdbsum/4xyi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4xyi ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/B6JV96_SCHJY B6JV96_SCHJY] 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 (By similarity).[SAAS:SAAS00349935] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | CENP-A is a centromere-specific histone H3 variant that is required for kinetochore assembly and accurate chromosome segregation. For it to function properly, CENP-A must be specifically localized to centromeres. In fission yeast, Scm3sp and the Mis18 complex, composed of Mis16, Eic1, and Mis18, function as a CENP-A(Cnp1)-specific chaperone and a recruiting factor, respectively, and together ensure accurate delivery of CENP-A(Cnp1) to centromeres. Although how Scm3sp specifically recognizes CENP-A(Cnp1) has been revealed recently, the recruiting mechanism of CENP-A(Cnp1) via the Mis18 complex remains unknown. In this study, we have determined crystal structures of Schizosaccharomyces japonicus Mis16 alone and in complex with the helix 1 of histone H4 (H4alpha1). Crystal structures followed by mutant analysis and affinity pull-downs have revealed that Mis16 recognizes both H4alpha1 and Scm3sp independently within the CENP-A(Cnp1)/H4:Scm3sp complex. This observation suggests that Mis16 gains CENP-A(Cnp1) specificity by recognizing both Scm3sp and histone H4. Our studies provide insights into the molecular mechanisms underlying specific recruitment of CENP-A(Cnp1)/H4:Scm3sp into centromeres. | ||
| - | + | Mis16 Independently Recognizes Histone H4 and the CENP-ACnp1-Specific Chaperone Scm3sp.,An S, Kim H, Cho US J Mol Biol. 2015 Oct 9;427(20):3230-40. doi: 10.1016/j.jmb.2015.08.022. Epub 2015, Sep 4. PMID:26343758<ref>PMID:26343758</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: An | + | <div class="pdbe-citations 4xyi" style="background-color:#fffaf0;"></div> |
| - | [[Category: Cho | + | == References == |
| - | [[Category: Kim | + | <references/> |
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Schizosaccharomyces japonicus yFS275]] | ||
| + | [[Category: An S]] | ||
| + | [[Category: Cho U-S]] | ||
| + | [[Category: Kim H]] | ||
Current revision
Mis16 with H4 peptide
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