8T0P

Structure of Cse4 bound to Ame1 and Okp1

Summary for 8T0P

• Entry DOI: 10.2210/pdb8t0p/pdb
• Descriptor: Inner kinetochore subunit AME1, Inner kinetochore subunit OKP1, Histone H3-like centromeric protein CSE4, ... (5 entities in total)
• Functional Keywords: okp1, cse4, ame1, kinetochore, cell cycle
• Biological source: Saccharomyces cerevisiae; More
• Total number of polymer chains: 3
• Total formula weight: 33766.47

Authors

Deng, S.,Harrison, S.C. (deposition date: 2023-06-01, release date: 2023-09-27, Last modification date: 2023-12-27)

Primary citation

Deng, S.,Cai, J.,Harrison, S.C.,Zhou, H.,Hinshaw, S.M.
Recognition of centromere-specific histone Cse4 by the inner kinetochore Okp1-Ame1 complex.
Embo Rep., 24:e57702-e57702, 2023

PubMed Abstract: Successful mitosis depends on the timely establishment of correct chromosomal attachments to microtubules. The kinetochore, a modular multiprotein complex, mediates this connection by recognizing specialized chromatin containing a histone H3 variant called Cse4 in budding yeast and CENP-A in vertebrates. Structural features of the kinetochore that enable discrimination between Cse4/CENP-A and H3 have been identified in several species. How and when these contribute to centromere recognition and how they relate to the overall structure of the inner kinetochore are unsettled questions. More generally, this molecular recognition ensures that only one kinetochore is built on each chromatid and that this happens at the right place on the chromatin fiber. We have determined the crystal structure of a Cse4 peptide bound to the essential inner kinetochore Okp1-Ame1 heterodimer from budding yeast. The structure and related experiments show in detail an essential point of Cse4 contact and provide information about the arrangement of the inner kinetochore.

PubMed: 37983946
DOI: 10.15252/embr.202357702

Experimental method

X-RAY DIFFRACTION (1.73 Å)