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| | <SX load='6gsa' size='340' side='right' viewer='molstar' caption='[[6gsa]], [[Resolution|resolution]] 4.20Å' scene=''> | | <SX load='6gsa' size='340' side='right' viewer='molstar' caption='[[6gsa]], [[Resolution|resolution]] 4.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6gsa]] is a 5 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6GSA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6GSA FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6gsa]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6GSA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6GSA FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6fe8|6fe8]]</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4.2Å</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=6gsa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6gsa OCA], [http://pdbe.org/6gsa PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6gsa RCSB], [http://www.ebi.ac.uk/pdbsum/6gsa PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6gsa ProSAT]</span></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=6gsa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6gsa OCA], [https://pdbe.org/6gsa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6gsa RCSB], [https://www.ebi.ac.uk/pdbsum/6gsa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6gsa ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CBF3A_YEAST CBF3A_YEAST]] Acts as a component of the centromere DNA-binding protein complex CBF3, which is essential for chromosome segregation and movement of centromeres along microtubules. CBF3 is required for the recruitment of other kinetochore complexes to CEN DNA. It plays a role in the attachment of chromosomes to the spindle and binds selectively to a highly conserved DNA sequence called CDEIII, found in centromers and in several promoters. [[http://www.uniprot.org/uniprot/CBF3B_YEAST CBF3B_YEAST]] Acts as a component of the centromere DNA-binding protein complex CBF3, which is essential for chromosome segregation and movement of centromeres along microtubules. CBF3 is required for the recruitment of other kinetochore complexes to CEN DNA. It plays a role in the attachment of chromosomes to the spindle and binds selectively to a highly conserved DNA sequence called CDEIII, found in centromers and in several promoters. [[http://www.uniprot.org/uniprot/CBF3C_YEAST CBF3C_YEAST]] Acts as central component of the centromere DNA-binding protein complex CBF3, which is essential for chromosome segregation and movement of centromeres along microtubules. CBF3 is required for the recruitment of other kinetochore complexes to CEN DNA. It plays a role in the attachment of chromosomes to the spindle and binds selectively to a highly conserved DNA sequence called CDEIII, found in centromers and in several promoters. The association of CBF3C with CBF3D and SGT1 is required for CBF3C activation and CBF3 assembly. [[http://www.uniprot.org/uniprot/SKP1_YEAST SKP1_YEAST]] Essential component of the E3 ubiquitin ligase complex SCF (SKP1-CUL1-F-box protein) ubiquitin ligase complex, which mediates the ubiquitination and subsequent proteasomal degradation of target proteins like phosphorylated SIC1. Participates in the attachment of chromosomes to the spindle. Acts as a regulatory component of the centromere DNA-binding protein complex CBF3, which is essential for chromosome segregation and movement of centromeres along microtubules. CBF3 is required for the recruitment of other kinetochore complexes to CEN DNA. It plays a role in the attachment of chromosomes to the spindle and binds selectively to a highly conserved DNA sequence called CDEIII, found in centromeres and in several promoters. The association of CBF3C with CBF3D and SGT1 is required for CBF3C activation and CBF3 assembly. SKP1/CBF3D could retrieve cyclins or cyclin-CDK-like proteins into the kinetochore thus providing cell cycle-regulated kinetochore activity. Involved in the regulation of methionine biosynthesis genes. Facilitates association of CDC53 with CDC4 and of ROY1 with YPT52.<ref>PMID:8706132</ref> <ref>PMID:8706131</ref> <ref>PMID:9346238</ref> <ref>PMID:9346239</ref> <ref>PMID:21389113</ref> <ref>PMID:9499404</ref> <ref>PMID:17517885</ref> | + | [https://www.uniprot.org/uniprot/CBF3B_YEAST CBF3B_YEAST] Acts as a component of the centromere DNA-binding protein complex CBF3, which is essential for chromosome segregation and movement of centromeres along microtubules. CBF3 is required for the recruitment of other kinetochore complexes to CEN DNA. It plays a role in the attachment of chromosomes to the spindle and binds selectively to a highly conserved DNA sequence called CDEIII, found in centromers and in several promoters. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </SX> | | </SX> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Lukoynova, N]] | + | [[Category: Saccharomyces cerevisiae]] |
| - | [[Category: Vaughan, C K]] | + | [[Category: Lukoynova N]] |
| - | [[Category: Zhang, W J]] | + | [[Category: Vaughan CK]] |
| - | [[Category: Cdeiii-binding]] | + | [[Category: Zhang WJ]] |
| - | [[Category: Centromere]]
| + | |
| - | [[Category: Dna binding protein]]
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| - | [[Category: Lrr domain]]
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| Structural highlights
Function
CBF3B_YEAST Acts as a component of the centromere DNA-binding protein complex CBF3, which is essential for chromosome segregation and movement of centromeres along microtubules. CBF3 is required for the recruitment of other kinetochore complexes to CEN DNA. It plays a role in the attachment of chromosomes to the spindle and binds selectively to a highly conserved DNA sequence called CDEIII, found in centromers and in several promoters.
Publication Abstract from PubMed
The centromere binding factor 3 (CBF3) complex binds the third centromere DNA element in organisms with point centromeres, such as S. cerevisiae. It is an essential complex for assembly of the kinetochore in these organisms, as it facilitates genetic centromere specification and allows association of all other kinetochore components. We determined high-resolution structures of the core complex of CBF3 alone and in association with a monomeric construct of Ndc10, using cryoelectron microscopy (cryo-EM). We identify the DNA-binding site of the complex and present a model in which CBF3 induces a tight bend in centromeric DNA, thus facilitating assembly of the centromeric nucleosome.
Insights into Centromere DNA Bending Revealed by the Cryo-EM Structure of the Core Centromere Binding Factor 3 with Ndc10.,Zhang W, Lukoynova N, Miah S, Lucas J, Vaughan CK Cell Rep. 2018 Jul 17;24(3):744-754. doi: 10.1016/j.celrep.2018.06.068. PMID:30021170[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Zhang W, Lukoynova N, Miah S, Lucas J, Vaughan CK. Insights into Centromere DNA Bending Revealed by the Cryo-EM Structure of the Core Centromere Binding Factor 3 with Ndc10. Cell Rep. 2018 Jul 17;24(3):744-754. doi: 10.1016/j.celrep.2018.06.068. PMID:30021170 doi:http://dx.doi.org/10.1016/j.celrep.2018.06.068
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