5OQN

Crystal structure of the S. cerevisiae condensin Ycg1-Brn1 subcomplex bound to DNA (short kleisin loop)

Summary for 5OQN

• Entry DOI: 10.2210/pdb5oqn/pdb
• Descriptor: Condensin complex subunit 3, Condensin complex subunit 2, DNA (5'-D(*GP*AP*TP*GP*TP*GP*TP*AP*GP*CP*TP*AP*CP*AP*CP*AP*TP*C)-3') (3 entities in total)
• Functional Keywords: kleisin, heat repeat, dna-binding, smc complex, cell cycle
• Biological source: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast); More
• Cellular location: Nucleus: Q06680 P38170
• Total number of polymer chains: 4
• Total formula weight: 125871.52

Authors

Kschonsak, M.,Hassler, M.,Haering, C.H. (deposition date: 2017-08-14, release date: 2017-10-18, Last modification date: 2024-01-17)

Primary citation

Kschonsak, M.,Merkel, F.,Bisht, S.,Metz, J.,Rybin, V.,Hassler, M.,Haering, C.H.
Structural Basis for a Safety-Belt Mechanism That Anchors Condensin to Chromosomes.
Cell, 171:588-600.e24, 2017

PubMed 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 HEAT-repeat and Brn1 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.

PubMed: 28988770
DOI: 10.1016/j.cell.2017.09.008

Experimental method

X-RAY DIFFRACTION (3.15 Å)