Summary information and primary citation

PDB-id
5oqp; DSSR-derived features in text and JSON formats
Class
cell cycle
Method
X-ray (2.98 Å)
Summary
Crystal structure of the s. cerevisiae condensin ycg1-brn1 subcomplex bound to DNA (crystal form i)
Reference
Kschonsak M, Merkel F, Bisht S, Metz J, Rybin V, Hassler M, Haering CH (2017): "Structural Basis for a Safety-Belt Mechanism That Anchors Condensin to Chromosomes." Cell, 171, 588-600.e24. doi: 10.1016/j.cell.2017.09.008.
Abstract
Condensin protein complexes coordinate the formation of mitotic chromosomes and thereby ensure the successful segregation of replicated genomes. Insights into how condensin complexes bind to chromosomes and alter their topology are essential for understanding the molecular principles behind the large-scale chromatin rearrangements that take place during cell divisions. Here, we identify a direct DNA-binding site in the eukaryotic condensin complex, which is formed by its Ycg1(Cnd3) HEAT-repeat and Brn1(Cnd2) kleisin subunits. DNA co-crystal structures reveal a conserved, positively charged groove that accommodates the DNA double helix. A peptide loop of the kleisin subunit encircles the bound DNA and, like a safety belt, prevents its dissociation. Firm closure of the kleisin loop around DNA is essential for the association of condensin complexes with chromosomes and their DNA-stimulated ATPase activity. Our data suggest a sophisticated molecular basis for anchoring condensin complexes to chromosomes that enables the formation of large-sized chromatin loops.

Cartoon-block schematics in six views (download the tarball)

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