4RSI

Yeast Smc2-Smc4 hinge domain with extended coiled coils

Summary for 4RSI

• Entry DOI: 10.2210/pdb4rsi/pdb
• Related: 4RSJ
• Descriptor: Structural maintenance of chromosomes protein 2, Structural maintenance of chromosomes protein 4, PHOSPHATE ION, ... (4 entities in total)
• Functional Keywords: smc hinge domain with coiled coil, chromosomal condensation, cell cycle
• Biological source: Saccharomyces cerevisiae (Baker's yeast); More
• Cellular location: Nucleus: P38989 Q12267
• Total number of polymer chains: 2
• Total formula weight: 90804.02

Authors

Soh, Y.M.,Shin, H.C.,Oh, B.H. (deposition date: 2014-11-08, release date: 2014-12-31, Last modification date: 2024-02-28)

Primary citation

Soh, Y.M.,Burmann, F.,Shin, H.C.,Oda, T.,Jin, K.S.,Toseland, C.P.,Kim, C.,Lee, H.,Kim, S.J.,Kong, M.S.,Durand-Diebold, M.L.,Kim, Y.G.,Kim, H.M.,Lee, N.K.,Sato, M.,Oh, B.H.,Gruber, S.
Molecular Basis for SMC Rod Formation and Its Dissolution upon DNA Binding.
Mol.Cell, 57:290-303, 2015

PubMed Abstract: SMC condensin complexes are central modulators of chromosome superstructure in all branches of life. Their SMC subunits form a long intramolecular coiled coil, which connects a constitutive "hinge" dimerization domain with an ATP-regulated "head" dimerization module. Here, we address the structural arrangement of the long coiled coils in SMC complexes. We unequivocally show that prokaryotic Smc-ScpAB, eukaryotic condensin, and possibly also cohesin form rod-like structures, with their coiled coils being closely juxtaposed and accurately anchored to the hinge. Upon ATP-induced binding of DNA to the hinge, however, Smc switches to a more open configuration. Our data suggest that a long-distance structural transition is transmitted from the Smc head domains to regulate Smc-ScpAB's association with DNA. These findings uncover a conserved architectural theme in SMC complexes, provide a mechanistic basis for Smc's dynamic engagement with chromosomes, and offer a molecular explanation for defects in Cornelia de Lange syndrome.

PubMed: 25557547
DOI: 10.1016/j.molcel.2014.11.023

Experimental method

X-RAY DIFFRACTION (2.9 Å)