5C6G

Structural Insights into the Scc2-Scc4 Cohesin Loader

Summary for 5C6G

• Entry DOI: 10.2210/pdb5c6g/pdb
• Descriptor: AGR133Cp, Sister chromatid cohesion protein 2 (3 entities in total)
• Functional Keywords: cohesin loader, tpr repeat, cell cycle
• Biological source: Ashbya gossypii (Yeast); More
• Cellular location: Nucleus : Q750S2
• Total number of polymer chains: 4
• Total formula weight: 190323.93

Authors

Singleton, M.R.,Chao, W.C.H. (deposition date: 2015-06-23, release date: 2015-08-05, Last modification date: 2024-05-08)

Primary citation

Chao, W.C.,Murayama, Y.,Munoz, S.,Costa, A.,Uhlmann, F.,Singleton, M.R.
Structural Studies Reveal the Functional Modularity of the Scc2-Scc4 Cohesin Loader.
Cell Rep, 12:719-725, 2015

PubMed Abstract: The remarkable accuracy of eukaryotic cell division is partly maintained by the cohesin complex acting as a molecular glue to prevent premature sister chromatid separation. The loading of cohesin onto chromosomes is catalyzed by the Scc2-Scc4 loader complex. Here, we report the crystal structure of Scc4 bound to the N terminus of Scc2 and show that Scc4 is a tetratricopeptide repeat (TPR) superhelix. The Scc2 N terminus adopts an extended conformation and is entrapped by the core of the Scc4 superhelix. Electron microscopy (EM) analysis reveals that the Scc2-Scc4 loader complex comprises three domains: a head, body, and hook. Deletion studies unambiguously assign the Scc2N-Scc4 as the globular head domain, whereas in vitro cohesin loading assays show that the central body and the hook domains are sufficient to catalyze cohesin loading onto circular DNA, but not chromatinized DNA in vivo, suggesting a possible role for Scc4 as a chromatin adaptor.

PubMed: 26212329
DOI: 10.1016/j.celrep.2015.06.071

Experimental method

X-RAY DIFFRACTION (2.6 Å)