7PB8
Crystal structure of the CENP-OPQUR complex
Summary for 7PB8
| Entry DOI | 10.2210/pdb7pb8/pdb |
| Descriptor | Centromere protein O, Centromere protein Q, Centromere protein U, ... (6 entities in total) |
| Functional Keywords | inner kinetochore, cell cycle |
| Biological source | Homo sapiens (human) More |
| Total number of polymer chains | 5 |
| Total formula weight | 151117.13 |
| Authors | Bellini, D.,Yatskevich, S.,Muir, K.W.,Barford, D. (deposition date: 2021-07-31, release date: 2022-04-27, Last modification date: 2024-01-31) |
| Primary citation | Yatskevich, S.,Muir, K.W.,Bellini, D.,Zhang, Z.,Yang, J.,Tischer, T.,Predin, M.,Dendooven, T.,McLaughlin, S.H.,Barford, D. Structure of the human inner kinetochore bound to a centromeric CENP-A nucleosome. Science, 376:844-852, 2022 Cited by PubMed Abstract: Kinetochores assemble onto specialized centromeric CENP-A (centromere protein A) nucleosomes (CENP-A) to mediate attachments between chromosomes and the mitotic spindle. We describe cryo-electron microscopy structures of the human inner kinetochore constitutive centromere associated network (CCAN) complex bound to CENP-A reconstituted onto α-satellite DNA. CCAN forms edge-on contacts with CENP-A, and a linker DNA segment of the α-satellite repeat emerges from the fully wrapped end of the nucleosome to thread through the central CENP-LN channel that tightly grips the DNA. The CENP-TWSX histone-fold module further augments DNA binding and partially wraps the linker DNA in a manner reminiscent of canonical nucleosomes. Our study suggests that the topological entrapment of the linker DNA by CCAN provides a robust mechanism by which kinetochores withstand both pushing and pulling forces exerted by the mitotic spindle. PubMed: 35420891DOI: 10.1126/science.abn3810 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.68 Å) |
Structure validation
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