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7Q2X

Cryo-EM structure of clamped S.cerevisiae condensin-DNA complex (Form I)

Summary for 7Q2X
Entry DOI10.2210/pdb7q2x/pdb
EMDB information13783
DescriptorStructural maintenance of chromosomes protein 2, Structural maintenance of chromosomes protein 4, Condensin complex subunit 2, ... (9 entities in total)
Functional Keywordscondensin, smc, cell cycle
Biological sourceSaccharomyces cerevisiae S288C
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Total number of polymer chains6
Total formula weight539173.24
Authors
Lee, B.-G.,Rhodes, J.,Lowe, J. (deposition date: 2021-10-26, release date: 2022-03-23, Last modification date: 2024-11-20)
Primary citationLee, B.G.,Rhodes, J.,Lowe, J.
Clamping of DNA shuts the condensin neck gate.
Proc.Natl.Acad.Sci.USA, 119:e2120006119-e2120006119, 2022
Cited by
PubMed Abstract: SignificanceDNA needs to be compacted to fit into nuclei and during cell division, when dense chromatids are formed for their mechanical segregation, a process that depends on the protein complex condensin. It forms and enlarges loops in DNA through loop extrusion. Our work resolves the atomic structure of a DNA-bound state of condensin in which ATP has not been hydrolyzed. The DNA is clamped within a compartment that has been reported previously in other structural maintenance of chromosomes (SMC) complexes, including Rad50, cohesin, and MukBEF. With the caveat of important differences, it means that all SMC complexes cycle through at least some similar states and undergo similar conformational changes in their head modules, while hydrolyzing ATP and translocating DNA.
PubMed: 35349345
DOI: 10.1073/pnas.2120006119
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3 Å)
Structure validation

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