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4XHL

Structure of S. cerevisiae Hrr25 1-394 (K38R mutant)

Summary for 4XHL
Entry DOI10.2210/pdb4xhl/pdb
Related4XH0 4XHG 4XHH
DescriptorCasein kinase I homolog HRR25, N-(2-AMINOETHYL)-5-CHLOROISOQUINOLINE-8-SULFONAMIDE, SULFATE ION, ... (4 entities in total)
Functional Keywordscasein kinase, monopolin, transferase-transferase inhibitor complex, transferase/transferase inhibitor
Biological sourceSaccharomyces cerevisiae (Baker's yeast)
Total number of polymer chains1
Total formula weight46892.76
Authors
Ye, Q.,Corbett, K.D. (deposition date: 2015-01-05, release date: 2016-01-06, Last modification date: 2023-09-27)
Primary citationYe, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.01 Å)
Structure validation

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數據於2025-06-11公開中

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