1W1W

Sc Smc1hd:Scc1-C complex, ATPgS

Summary for 1W1W

• Entry DOI: 10.2210/pdb1w1w/pdb
• Descriptor: STRUCTURAL MAINTENANCE OF CHROMOSOME 1, SISTER CHROMATID COHESION PROTEIN 1, MAGNESIUM ION, ... (4 entities in total)
• Functional Keywords: cohesin, chromosome segregation, cell adhesion, kleisin, mitosis, cell cycle
• Biological source: SACCHAROMYCES CEREVISIAE (BAKER'S YEAST); More
• Total number of polymer chains: 8
• Total formula weight: 252596.66

Authors

Haering, C.,Nasmyth, K.,Lowe, J. (deposition date: 2004-06-24, release date: 2004-09-30, Last modification date: 2024-05-08)

Primary citation

Haering, C.H.,Schoffnegger, D.,Nishino, T.,Helmhart, W.,Nasmyth, K.,Lowe, J.
Structure and stability of cohesin's Smc1-kleisin interaction.
Mol. Cell, 15:951-964, 2004

PubMed Abstract: A multisubunit complex called cohesin forms a huge ring structure that mediates sister chromatid cohesion, possibly by entrapping sister DNAs following replication. Cohesin's kleisin subunit Scc1 completes the ring, connecting the ABC-like ATPase heads of a V-shaped Smc1/3 heterodimer. Proteolytic cleavage of Scc1 by separase triggers sister chromatid disjunction, presumably by breaking the Scc1 bridge. One half of the SMC-kleisin bridge is revealed here by a crystal structure of Smc1's ATPase complexed with Scc1's C-terminal domain. The latter forms a winged helix that binds a pair of beta strands in Smc1's ATPase head. Mutation of conserved residues within the contact interface destroys Scc1's interaction with Smc1/3 heterodimers and eliminates cohesin function. Interaction of Scc1's N terminus with Smc3 depends on prior C terminus connection with Smc1. There is little or no turnover of Smc1-Scc1 interactions within cohesin complexes in vivo because expression of noncleavable Scc1 after DNA replication does not hinder anaphase.

PubMed: 15383284
DOI: 10.1016/j.molcel.2004.08.030

Experimental method

X-RAY DIFFRACTION (2.9 Å)