4D2U
Negative-stain electron microscopy of E. coli ClpB (BAP form bound to ClpP)
Summary for 4D2U
Entry DOI | 10.2210/pdb4d2u/pdb |
Related | 4D2Q |
EMDB information | 2557 |
Descriptor | CHAPERONE PROTEIN CLPB (1 entity in total) |
Functional Keywords | chaperone, disaggregase, wild type, coiled-coil domain |
Biological source | ESCHERICHIA COLI |
Cellular location | Cytoplasm : P63284 |
Total number of polymer chains | 6 |
Total formula weight | 581010.52 |
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: 2014-05-13, release date: 2014-06-04, Last modification date: 2017-08-23) |
Primary citation | 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 Cited by PubMed: 24843029DOI: 10.7554/ELIFE.02481 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (17 Å) |
Structure validation
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