2l5a

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==Structural basis for recognition of centromere specific histone H3 variant by nonhistone Scm3==
==Structural basis for recognition of centromere specific histone H3 variant by nonhistone Scm3==
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<StructureSection load='2l5a' size='340' side='right' caption='[[2l5a]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
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<StructureSection load='2l5a' size='340' side='right'caption='[[2l5a]]' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2l5a]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L5A OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2L5A FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2l5a]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L5A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2L5A FirstGlance]. <br>
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</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CSE4, CSL2, YKL049C, YKL262, SCM3, YDL139C, D2155, HHF1, YBR009C, YBR0122, HHF2, YNL030W, N2752 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])</td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<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=2l5a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l5a OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2l5a RCSB], [http://www.ebi.ac.uk/pdbsum/2l5a PDBsum]</span></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=2l5a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l5a OCA], [https://pdbe.org/2l5a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2l5a RCSB], [https://www.ebi.ac.uk/pdbsum/2l5a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2l5a ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/CENPA_YEAST CENPA_YEAST]] Histone H3-like variant which exclusively replaces conventional H3 in the nucleosome core of centromeric chromatin at the inner plate of the kinetochore. Required for recruitment and assembly of kinetochore proteins, mitotic progression and chromosome segregation. May serve as an epigenetic mark that propagates centromere identity through replication and cell division. Required for functional chromatin architecture at the yeast 2-micron circle partitioning locus and promotes equal plasmid segregation.<ref>PMID:7698647</ref> <ref>PMID:9741625</ref> <ref>PMID:9584087</ref> <ref>PMID:10454560</ref> <ref>PMID:11063678</ref> <ref>PMID:10891506</ref> <ref>PMID:10499801</ref> <ref>PMID:11606525</ref> <ref>PMID:15590827</ref> <ref>PMID:16207811</ref> <ref>PMID:16966420</ref>
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[https://www.uniprot.org/uniprot/SCM3_YEAST SCM3_YEAST] Centromeric protein that plays a central role in the incorporation and maintenance of histone H3-like variant CENPA at centromeres.[UniProtKB:Q8NCD3][https://www.uniprot.org/uniprot/CENPA_YEAST CENPA_YEAST] Histone H3-like variant which exclusively replaces conventional H3 in the nucleosome core of centromeric chromatin at the inner plate of the kinetochore. Required for recruitment and assembly of kinetochore proteins, mitotic progression and chromosome segregation. May serve as an epigenetic mark that propagates centromere identity through replication and cell division. Required for functional chromatin architecture at the yeast 2-micron circle partitioning locus and promotes equal plasmid segregation.<ref>PMID:7698647</ref> <ref>PMID:9741625</ref> <ref>PMID:9584087</ref> <ref>PMID:10454560</ref> <ref>PMID:11063678</ref> <ref>PMID:10891506</ref> <ref>PMID:10499801</ref> <ref>PMID:11606525</ref> <ref>PMID:15590827</ref> <ref>PMID:16207811</ref> <ref>PMID:16966420</ref> [https://www.uniprot.org/uniprot/H4_YEAST H4_YEAST]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The centromere is a unique chromosomal locus that ensures accurate segregation of chromosomes during cell division by directing the assembly of a multiprotein complex, the kinetochore. The centromere is marked by a conserved variant of conventional histone H3 termed CenH3 or CENP-A (ref. 2). A conserved motif of CenH3, the CATD, defined by loop 1 and helix 2 of the histone fold, is necessary and sufficient for specifying centromere functions of CenH3 (refs 3, 4). The structural basis of this specification is of particular interest. Yeast Scm3 and human HJURP are conserved non-histone proteins that interact physically with the (CenH3-H4)(2) heterotetramer and are required for the deposition of CenH3 at centromeres in vivo. Here we have elucidated the structural basis for recognition of budding yeast (Saccharomyces cerevisiae) CenH3 (called Cse4) by Scm3. We solved the structure of the Cse4-binding domain (CBD) of Scm3 in complex with Cse4 and H4 in a single chain model. An alpha-helix and an irregular loop at the conserved amino terminus and a shorter alpha-helix at the carboxy terminus of Scm3(CBD) wraps around the Cse4-H4 dimer. Four Cse4-specific residues in the N-terminal region of helix 2 are sufficient for specific recognition by conserved and functionally important residues in the N-terminal helix of Scm3 through formation of a hydrophobic cluster. Scm3(CBD) induces major conformational changes and sterically occludes DNA-binding sites in the structure of Cse4 and H4. These findings have implications for the assembly and architecture of the centromeric nucleosome.
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Structural basis for recognition of centromere histone variant CenH3 by the chaperone Scm3.,Zhou Z, Feng H, Zhou BR, Ghirlando R, Hu K, Zwolak A, Miller Jenkins LM, Xiao H, Tjandra N, Wu C, Bai Y Nature. 2011 Apr 14;472(7342):234-7. Epub 2011 Mar 16. PMID:21412236<ref>PMID:21412236</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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==See Also==
==See Also==
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*[[Histone|Histone]]
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*[[Histone 3D structures|Histone 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
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[[Category: Bai, Y]]
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[[Category: Bai Y]]
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[[Category: Feng, H]]
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[[Category: Feng H]]
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[[Category: Ghirlando, R]]
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[[Category: Ghirlando R]]
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[[Category: Hu, K]]
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[[Category: Hu K]]
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[[Category: Jenkins, L]]
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[[Category: Jenkins L]]
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[[Category: Tjandra, N]]
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[[Category: Tjandra N]]
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[[Category: Wu, C]]
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[[Category: Wu C]]
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[[Category: Xiao, H]]
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[[Category: Xiao H]]
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[[Category: Zhou, B]]
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[[Category: Zhou B]]
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[[Category: Zhou, Z]]
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[[Category: Zhou Z]]
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[[Category: Zwolak, A]]
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[[Category: Zwolak A]]
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[[Category: A single chain of cse4+scm3+h4]]
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[[Category: Chimera protein]]
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[[Category: Fusion protein]]
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[[Category: Nuclear protein]]
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Current revision

Structural basis for recognition of centromere specific histone H3 variant by nonhistone Scm3

PDB ID 2l5a

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