6o2k

<table><tr><td colspan='2'>[[6o2k]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Drome Drome]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6O2K OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6O2K FirstGlance]. <br>

</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Cenp-C, CENP-C, cenp-C, Cenp-C-RA, CenpC, CG11745, CG11746, CLD1, Dmel\CG31258, l(2)SH3 157, l(3)85Aa, l(3)SH157, L1, CG31258, Dmel_CG31258 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 DROME])</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=6o2k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6o2k OCA], [http://pdbe.org/6o2k PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6o2k RCSB], [http://www.ebi.ac.uk/pdbsum/6o2k PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6o2k ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

The successful assembly and regulation of the kinetochore are critical for the equal and accurate segregation of genetic material during the cell cycle. CENP-C (centromere protein C), a conserved inner kinetochore component, has been broadly characterized as a scaffolding protein and is required for the recruitment of multiple kinetochore proteins to the centromere. At its C terminus, CENP-C harbors a conserved cupin domain that has an established role in protein dimerization. Although the crystal structure of the Saccharomyces cerevisiae Mif2(CENP-C) cupin domain has been determined, centromeric organization and kinetochore composition vary greatly between S. cerevisiae (point centromere) and other eukaryotes (regional centromere). Therefore, whether the structural and functional role of the cupin domain is conserved throughout evolution requires investigation. Here, we report the crystal structures of the Schizosaccharomyces pombe and Drosophila melanogaster CENP-C cupin domains at 2.52 and 1.81 A resolutions, respectively. Although the central jelly roll architecture is conserved among the three determined CENP-C cupin domain structures, the cupin domains from organisms with regional centromeres contain additional structural features that aid in dimerization. Moreover, we found that the S. pombe Cnp3(CENP-C) jelly roll fold harbors an inner binding pocket that is used to recruit the meiosis-specific protein Moa1. In summary, our results unveil the evolutionarily conserved and unique features of the CENP-C cupin domain and uncover the mechanism by which it functions as a recruitment factor.

 

== References ==

[[Category: Drome]]

[[Category: Chik, J K]]

[[Category: Cho, U S]]

[[Category: Kinetochore]]