5CYZ

Structure of S. cerevisiae Hrr25:Mam1 complex, form 1

Summary for 5CYZ

• Entry DOI: 10.2210/pdb5cyz/pdb
• Descriptor: Casein kinase I homolog HRR25, Monopolin complex subunit MAM1, ZINC ION, ... (4 entities in total)
• Functional Keywords: casein kinase, monopolin, transferase
• Biological source: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast); More
• Total number of polymer chains: 2
• Total formula weight: 59407.46

Authors

Ye, Q.,Corbett, K.D. (deposition date: 2015-07-31, release date: 2016-08-03, Last modification date: 2023-09-27)

Primary citation

Ye, Q.,Ur, S.N.,Su, T.Y.,Corbett, K.D.
Structure of the Saccharomyces cerevisiae Hrr25:Mam1 monopolin subcomplex reveals a novel kinase regulator.
Embo J., 35:2139-2151, 2016

PubMed Abstract: In budding yeast, the monopolin complex mediates sister kinetochore cross-linking and co-orientation in meiosis I. The CK1δ kinase Hrr25 is critical for sister kinetochore co-orientation, but its roles are not well understood. Here, we present the structures of Hrr25 and its complex with the monopolin subunit Mam1. Hrr25 possesses a "central domain" that packs tightly against the kinase C-lobe, adjacent to the binding site for Mam1. Together, the Hrr25 central domain and Mam1 form a novel, contiguous embellishment to the Hrr25 kinase domain that affects Hrr25 conformational dynamics and enzyme kinetics. Mam1 binds a hydrophobic surface on the Hrr25 N-lobe that is conserved in CK1δ-family kinases, suggesting a role for this surface in recruitment and/or regulation of these enzymes throughout eukaryotes. Finally, using purified proteins, we find that Hrr25 phosphorylates the kinetochore receptor for monopolin, Dsn1. Together with our new structural insights into the fully assembled monopolin complex, this finding suggests that tightly localized Hrr25 activity modulates monopolin complex-kinetochore interactions through phosphorylation of both kinetochore and monopolin complex components.

PubMed: 27491543
DOI: 10.15252/embj.201694082

Experimental method

X-RAY DIFFRACTION (1.841 Å)