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-Structure paper
タイトル | Architecture and Nucleotide-Dependent Conformational Changes of the Rvb1-Rvb2 AAA+ Complex Revealed by Cryoelectron Microscopy. |
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ジャーナル・号・ページ | Structure, Vol. 24, Issue 5, Page 657-666, Year 2016 |
掲載日 | 2016年5月3日 |
著者 | Caroline A Ewens / Min Su / Liang Zhao / Nardin Nano / Walid A Houry / Daniel R Southworth / |
PubMed 要旨 | Rvb1 and Rvb2 are essential AAA+ proteins that interact together during the assembly and activity of diverse macromolecules including chromatin remodelers INO80 and SWR-C, and ribonucleoprotein ...Rvb1 and Rvb2 are essential AAA+ proteins that interact together during the assembly and activity of diverse macromolecules including chromatin remodelers INO80 and SWR-C, and ribonucleoprotein complexes including telomerase and snoRNPs. ATP hydrolysis by Rvb1/2 is required for function; however, the mechanism that drives substrate remodeling is unknown. Here we determined the architecture of the yeast Rvb1/2 dodecamer using cryoelectron microscopy and identify that the substrate-binding insertion domain undergoes conformational changes in response to nucleotide state. 2D and 3D classification defines the dodecamer flexibility, revealing distinct arrangements and the hexamer-hexamer interaction interface. Reconstructions of the apo, ATP, and ADP states identify that Rvb1/2 undergoes substantial conformational changes that include a twist in the insertion-domain position and a corresponding rotation of the AAA+ ring. These results reveal how the ATP hydrolysis cycle of the AAA+ domains directs insertion-domain movements that could provide mechanical force during remodeling or helicase activities. |
リンク | Structure / PubMed:27112599 |
手法 | EM (単粒子) |
解像度 | 6.4 - 9.5 Å |
構造データ | EMDB-3080: EMDB-3081: EMDB-3082: EMDB-3083: EMDB-3084: EMDB-3085: |
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