1w1w

From Proteopedia

Revision as of 15:17, 5 November 2007

SC SMC1HD:SCC1-C COMPLEX, ATPGS

Overview

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.

About this Structure

1W1W is a Protein complex structure of sequences from Saccharomyces cerevisiae with MG and ATG as ligands. Structure known Active Site: AC1. Full crystallographic information is available from OCA.

Reference

Structure and stability of cohesin's Smc1-kleisin interaction., Haering CH, Schoffnegger D, Nishino T, Helmhart W, Nasmyth K, Lowe J, Mol Cell. 2004 Sep 24;15(6):951-64. PMID:15383284

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