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5KTB

Structure of a complex between S. cerevisiae Csm1 and Mam1

Replaces:  4EMC
Summary for 5KTB
Entry DOI10.2210/pdb5ktb/pdb
DescriptorMonopolin complex subunit CSM1, Monopolin complex subunit MAM1 (2 entities in total)
Functional Keywordsmonopolin, replication
Biological sourceSaccharomyces cerevisiae (Baker's yeast)
More
Total number of polymer chains3
Total formula weight51595.14
Authors
Corbett, K.D.,Harrison, S.C. (deposition date: 2016-07-11, release date: 2016-07-20, Last modification date: 2023-10-04)
Primary citationCorbett, K.D.,Harrison, S.C.
Molecular architecture of the yeast monopolin complex.
Cell Rep, 1:583-589, 2012
Cited by
PubMed Abstract: The Saccharomyces cerevisiae monopolin complex directs proper chromosome segregation in meiosis I by mediating co-orientation of sister kinetochores on the meiosis I spindle. The monopolin subunits Csm1 and Lrs4 form a V-shaped complex that may directly crosslink sister kinetochores. We report here biochemical characterization of the monopolin complex subunits Mam1 and Hrr25 and of the complete four-protein monopolin complex. By purifying monopolin subcomplexes with different subunit combinations, we have determined the stoichiometry and overall architecture of the full monopolin complex. We have determined the crystal structure of Csm1 bound to a Mam1 fragment, showing how Mam1 wraps around the Csm1 dimer and alters the stoichiometry of kinetochore-protein binding by Csm1. We further show that the kinase activity of Hrr25 is altered by Mam1 binding, and we identify Hrr25 phosphorylation sites on Mam1 that may affect monopolin complex stability and/or kinetochore binding in meiosis.
PubMed: 22813733
DOI: 10.1016/j.celrep.2012.05.012
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.05 Å)
Structure validation

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