9OKE
Structure of the Bombyx mori bmCENP-HIKM-LN-T-OP complex without the CS module
Summary for 9OKE
| Entry DOI | 10.2210/pdb9oke/pdb |
| Related | 9OKB 9OKD |
| EMDB information | 70561 |
| Descriptor | bmCENP-H, bmCENP-K, Centromere protein I, ... (9 entities in total) |
| Functional Keywords | ccan, complex, segregation, dna binding protein |
| Biological source | Bombyx mori (domestic silkworm) More |
| Total number of polymer chains | 9 |
| Total formula weight | 445232.41 |
| Authors | |
| Primary citation | Yu, C.,Sankaranarayanan, S.R.,Cornilleau, G.,Howes, A.C.,Azumaya, C.M.,Day, E.S.,Zilberleyb, I.,Brillantes, B.,Cheung, T.K.,Dec, L.,Loew, D.,Tran, P.,Rose, C.M.,Drinnenberg, I.A.,Ciferri, C.,Yatskevich, S. Architecture and function of holocentric CENP-A-independent inner kinetochores. Sci Adv, 12:eaeb5817-eaeb5817, 2026 Cited by PubMed Abstract: Kinetochores are essential macromolecular complexes anchoring chromosomes to the mitotic spindle, ensuring faithful cell division. Despite their critical role, the structural organization of kinetochores across diverse species remains poorly understood. We present the inner kinetochore constitutive centromere-associated network (CCAN) structure of the silkmoth , an insect that lacks the canonical centromere-specifying histone variant CENP-A and exhibits chromosome-wide centromeric activity (holocentric). The CCAN incorporates four previously uncharacterized centromeric subunit proteins that are structurally related to the Dam1/DASH complex but function in scaffolding the inner kinetochore rather than in microtubule binding. Similar to the yeast and human systems, the CCAN also entraps DNA within its central closed chamber. However, unlike these systems, the CCAN can also assemble in vitro into a self-contained head-to-head dimer via atypical histone-fold protein dimerization. On the basis of our findings, we propose that the holocentric organization may emerge from the modular arrangement of discrete kinetochore units. PubMed: 42319948DOI: 10.1126/sciadv.aeb5817 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.24 Å) |
Structure validation
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