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4D2Q

Negative-stain electron microscopy of E. coli ClpB mutant E432A (BAP form bound to ClpP)

Summary for 4D2Q
Entry DOI10.2210/pdb4d2q/pdb
Related4D2U 4D2X
EMDB information2555
DescriptorCLPB (1 entity in total)
Functional Keywordschaperone, disaggregase, clpb, bap, coiled-coil domain
Biological sourceESCHERICHIA COLI
Cellular locationCytoplasm : P63284
Total number of polymer chains6
Total formula weight581010.52
Authors
Carroni, M.,Kummer, E.,Oguchi, Y.,Clare, D.K.,Wendler, P.,Sinning, I.,Kopp, J.,Mogk, A.,Bukau, B.,Saibil, H.R. (deposition date: 2014-05-12, release date: 2014-06-04, Last modification date: 2017-08-23)
Primary citationCarroni, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (18 Å)
Structure validation

226707

数据于2024-10-30公开中

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