4D2X

Negative-stain electron microscopy of E. coli ClpB of Y503D hyperactive mutant (BAP form bound to ClpP)

4D2X の概要

• エントリーDOI: 10.2210/pdb4d2x/pdb
• 関連するPDBエントリー: 4D2Q 4D2U
• EMDBエントリー: 2559
• 分子名称: CHAPERONE PROTEIN CLPB (1 entity in total)
• 機能のキーワード: chaperone, disaggregase, clpb, bap, y503d hyperactive mutant, coiled- coil domain
• 由来する生物種: ESCHERICHIA COLI
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 581010.52

構造登録者

Carroni, M.,Kummer, E.,Oguchi, Y.,Clare, D.K.,Wendler, P.,Sinning, I.,Kopp, J.,Mogk, A.,Bukau, B.,Saibil, H.R. (登録日: 2014-05-13, 公開日: 2014-06-04, 最終更新日: 2024-10-16)

主引用文献

Carroni, M.,Kummer, E.,Oguchi, Y.,Wendler, P.,Clare, D.K.,Sinning, I.,Kopp, J.,Mogk, A.,Bukau, B.,Saibil, H.R.
Head-to-Tail Interactions of the Coiled-Coil Domains Regulate Clpb Activity and Cooperation with Hsp70 in Protein Disaggregation.
Elife, 3:02481-, 2014

PubMed Abstract: 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.

PubMed: 24843029
DOI: 10.7554/ELIFE.02481

実験手法

ELECTRON MICROSCOPY (20 Å)