4IT3
Crystal Structure of Iml3 from S. cerevisiae
Summary for 4IT3
| Entry DOI | 10.2210/pdb4it3/pdb |
| Related | 4JE3 |
| Descriptor | Central kinetochore subunit IML3 (2 entities in total) |
| Functional Keywords | beta sheet, kinetochore, chl4, nucleus, cell cycle |
| Biological source | Saccharomyces cerevisiae (Baker's yeast) |
| Cellular location | Nucleus: P38265 |
| Total number of polymer chains | 1 |
| Total formula weight | 28787.53 |
| Authors | Hinshaw, S.M.,Harrison, S.C. (deposition date: 2013-01-17, release date: 2013-10-16, Last modification date: 2024-10-30) |
| Primary citation | Hinshaw, S.M.,Harrison, S.C. An iml3-chl4 heterodimer links the core centromere to factors required for accurate chromosome segregation. Cell Rep, 5:29-36, 2013 Cited by PubMed Abstract: Accurate segregation of genetic material in eukaryotes relies on the kinetochore, a multiprotein complex that connects centromeric DNA with microtubules. In yeast and humans, two proteins-Mif2/CENP-C and Chl4/CNEP-N-interact with specialized centromeric nucleosomes and establish distinct but cross-connecting axes of chromatin-microtubule linkage. Proteins recruited by Chl4/CENP-N include a subset that regulates chromosome transmission fidelity. We show that Chl4 and a conserved member of this subset, Iml3, both from Saccharomyces cerevisiae, form a stable protein complex that interacts with Mif2 and Sgo1. We have determined the structures of an Iml3 homodimer and an Iml3-Chl4 heterodimer, which suggest a mechanism for regulating the assembly of this functional axis of the kinetochore. We propose that at the core centromere, the Chl4-Iml3 complex participates in recruiting factors, such as Sgo1, that influence sister chromatid cohesion and encourage sister kinetochore biorientation. PubMed: 24075991DOI: 10.1016/j.celrep.2013.08.036 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.495 Å) |
Structure validation
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