4aco: Difference between revisions
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==Structure of the budding yeast Ndc10 N-terminal domain== | ==Structure of the budding yeast Ndc10 N-terminal domain== | ||
<StructureSection load='4aco' size='340' side='right' caption='[[4aco]], [[Resolution|resolution]] 1.89Å' scene=''> | <StructureSection load='4aco' size='340' side='right'caption='[[4aco]], [[Resolution|resolution]] 1.89Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4aco]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4aco]] is a 1 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=4ACO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ACO FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.89Å</td></tr> | ||
<table> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4aco FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4aco OCA], [https://pdbe.org/4aco PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4aco RCSB], [https://www.ebi.ac.uk/pdbsum/4aco PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4aco ProSAT]</span></td></tr> | ||
</table> | |||
== Function == | |||
[https://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. | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 4aco" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Centromere protein 3D structure|Centromere protein 3D structure]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: Perriches | [[Category: Perriches T]] | ||
[[Category: Singleton | [[Category: Singleton MR]] | ||
Latest revision as of 13:49, 9 May 2024
Structure of the budding yeast Ndc10 N-terminal domainStructure of the budding yeast Ndc10 N-terminal domain
Structural highlights
FunctionCBF3A_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 PubMedWe have solved the X-ray structure of the amino-terminal half of the yeast kinetochore protein Ndc10 at 1.8 Angstrom resolution. This essential protein is a key constituent of the budding yeast centromere, and is essential for the recruitment of the centromeric nucleosome and establishment of the kinetochore. The fold of the protein shows unexpected similarities to the tyrosine recombinase/lambda-integrase family of proteins, most notably Cre, with some variation in the relative position of the sub-domains. This finding offers new insights into kinetochore evolution and the adaptation of a well-studied protein fold to a novel role. By comparison to tyrosine recombinases, and mutagenesis studies, we have been able to define some of the key DNA-binding motifs. The structure of the yeast kinetochore Ndc10 DNA-binding domain reveals an unexpected evolutionary relationship to tyrosine recombinases.,Perriches T, Singleton MR J Biol Chem. 2012 Jan 3. PMID:22215672[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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