4UX3

cohesin Smc3-HD:Scc1-N complex from yeast

Summary for 4UX3

• Entry DOI: 10.2210/pdb4ux3/pdb
• Descriptor: STRUCTURAL MAINTENANCE OF CHROMOSOMES PROTEIN 3, MITOTIC CHROMOSOME DETERMINANT-RELATED PROTEIN, MAGNESIUM ION, ... (4 entities in total)
• Functional Keywords: protein binding, cohesin, mitosis, chromosome segregation, kleisin, smc
• Biological source: SACCHAROMYCES CEREVISIAE (BAKER'S YEAST); More
• Cellular location: Nucleus: P47037
• Total number of polymer chains: 2
• Total formula weight: 76108.76

Authors

Gligoris, T.G.,Nasmyth, K.,Lowe, J. (deposition date: 2014-08-18, release date: 2014-12-03, Last modification date: 2024-01-10)

Primary citation

Gligoris, T.G.,Scheinost, J.C.,Burmann, F.,Petela, N.,Chan, K.,Uluocak, P.,Beckouet, F.,Gruber, S.,Nasmyth, K.,Lowe, J.
Closing the Cohesin Ring: Structure and Function of its Smc3-Kleisin Interface.
Science, 346:963-, 2014

PubMed Abstract: Through their association with a kleisin subunit (Scc1), cohesin's Smc1 and Smc3 subunits are thought to form tripartite rings that mediate sister chromatid cohesion. Unlike the structure of Smc1/Smc3 and Smc1/Scc1 interfaces, that of Smc3/Scc1 is not known. Disconnection of this interface is thought to release cohesin from chromosomes in a process regulated by acetylation. We show here that the N-terminal domain of yeast Scc1 contains two α helices, forming a four-helix bundle with the coiled coil emerging from Smc3's adenosine triphosphatase head. Mutations affecting this interaction compromise cohesin's association with chromosomes. The interface is far from Smc3 residues, whose acetylation prevents cohesin's dissociation from chromosomes. Cohesin complexes holding chromatids together in vivo do indeed have the configuration of hetero-trimeric rings, and sister DNAs are entrapped within these.

PubMed: 25414305
DOI: 10.1126/SCIENCE.1256917

Experimental method

X-RAY DIFFRACTION (3.3 Å)