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-Structure paper
タイトル | Head-to-tail interactions of the coiled-coil domains regulate ClpB activity and cooperation with Hsp70 in protein disaggregation. |
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ジャーナル・号・ページ | Elife, Vol. 3, Page e02481, Year 2014 |
掲載日 | 2014年4月30日 |
著者 | Marta Carroni / Eva Kummer / Yuki Oguchi / Petra Wendler / Daniel K Clare / Irmgard Sinning / Jürgen Kopp / Axel Mogk / Bernd Bukau / Helen R Saibil / |
PubMed 要旨 | The hexameric AAA+ chaperone ClpB reactivates aggregated proteins in cooperation with the Hsp70 system. Essential for disaggregation, the ClpB middle domain (MD) is a coiled-coil propeller that binds ...The hexameric AAA+ chaperone ClpB reactivates aggregated proteins in cooperation with the Hsp70 system. Essential for disaggregation, the ClpB middle domain (MD) is a coiled-coil propeller that binds Hsp70. Although the ClpB subunit structure is known, positioning of the MD in the hexamer and its mechanism of action are unclear. We obtained electron microscopy (EM) structures of the BAP variant of ClpB that binds the protease ClpP, clearly revealing MD density on the surface of the ClpB ring. Mutant analysis and asymmetric reconstructions show that MDs adopt diverse positions in a single ClpB hexamer. Adjacent, horizontally oriented MDs form head-to-tail contacts and repress ClpB activity by preventing Hsp70 interaction. Tilting of the MD breaks this contact, allowing Hsp70 binding, and releasing the contact in adjacent subunits. Our data suggest a wavelike activation of ClpB subunits around the ring.DOI: http://dx.doi.org/10.7554/eLife.02481.001. |
リンク | Elife / PubMed:24843029 / PubMed Central |
手法 | EM (単粒子) / X線回折 |
解像度 | 3.5 - 29.0 Å |
構造データ | EMDB-2555, PDB-4d2q: EMDB-2556: EMDB-2557, PDB-4d2u: EMDB-2558: EMDB-2559: Negative-stain electron microscopy of E. coli ClpB (BAP form bound to ClpP) EMDB-2560: EMDB-2561: EMDB-2562: EMDB-2563: PDB-4ciu: |
化合物 | ChemComp-ADP: |
由来 |
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キーワード | CHAPERONE / AAA+ / ATPASE / DISAGGREGASE / CLPB / BAP / COILED-COIL DOMAIN / WILD TYPE / Y503D HYPERACTIVE MUTANT / COILED- COIL DOMAIN |