6C0W
Cryo-EM structure of human kinetochore protein CENP-N with the centromeric nucleosome containing CENP-A
Summary for 6C0W
| Entry DOI | 10.2210/pdb6c0w/pdb |
| Related | 6EQT |
| EMDB information | 7326 |
| Descriptor | Histone H3-like centromeric protein A, Histone H4, Histone H2A, ... (7 entities in total) |
| Functional Keywords | nucleosome, cenp-a, kinetochore, cenp-n, structural protein-dna complex, structural protein/dna |
| Biological source | Homo sapiens (Human) More |
| Total number of polymer chains | 11 |
| Total formula weight | 236486.00 |
| Authors | Zhou, K.,Pentakota, S.,Vetter, I.R.,Morgan, G.P.,Petrovic, A.,Musacchio, A.,Luger, K. (deposition date: 2018-01-02, release date: 2018-01-17, Last modification date: 2024-03-13) |
| Primary citation | Pentakota, S.,Zhou, K.,Smith, C.,Maffini, S.,Petrovic, A.,Morgan, G.P.,Weir, J.R.,Vetter, I.R.,Musacchio, A.,Luger, K. Decoding the centromeric nucleosome through CENP-N. Elife, 6:-, 2017 Cited by PubMed Abstract: Centromere protein (CENP) A, a histone H3 variant, is a key epigenetic determinant of chromosome domains known as centromeres. Centromeres nucleate kinetochores, multi-subunit complexes that capture spindle microtubules to promote chromosome segregation during mitosis. Two kinetochore proteins, CENP-C and CENP-N, recognize CENP-A in the context of a rare CENP-A nucleosome. Here, we reveal the structural basis for the exquisite selectivity of CENP-N for centromeres. CENP-N uses charge and space complementarity to decode the L1 loop that is unique to CENP-A. It also engages in extensive interactions with a 15-base pair segment of the distorted nucleosomal DNA double helix, in a position predicted to exclude chromatin remodelling enzymes. Besides CENP-A, stable centromere recruitment of CENP-N requires a coincident interaction with a newly identified binding motif on nucleosome-bound CENP-C. Collectively, our studies clarify how CENP-N and CENP-C decode and stabilize the non-canonical CENP-A nucleosome to enforce epigenetic centromere specification and kinetochore assembly. PubMed: 29280735DOI: 10.7554/eLife.33442 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4 Å) |
Structure validation
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