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-Structure paper
タイトル | Clamping of DNA shuts the condensin neck gate. |
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ジャーナル・号・ページ | Proc Natl Acad Sci U S A, Vol. 119, Issue 14, Page e2120006119, Year 2022 |
掲載日 | 2022年4月5日 |
著者 | Byung-Gil Lee / James Rhodes / Jan Löwe / |
PubMed 要旨 | 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 ...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. |
リンク | Proc Natl Acad Sci U S A / PubMed:35349345 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 3.0 - 9.0 Å |
構造データ | EMDB-13783, PDB-7q2x: EMDB-13784, PDB-7q2y: EMDB-13785: Cryo-EM map of clamped S.cerevisiae condensin-DNA complex (pentamer dataset) EMDB-13786, PDB-7q2z: EMDB-13787: Cryo-EM map of clamped S.cerevisiae condensin complex on circular DNA EMDB-13788: Cryo-EM map of S.cerevisiae condensin Ycg1-Brn1 complex on circular DNA |
化合物 | ChemComp-ADP: ChemComp-BEF: ChemComp-MG: |
由来 |
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キーワード | CELL CYCLE / condensin / SMC / Ycg1 / heat repeat / HAWK |