4B9Q
Open conformation of ATP-bound Hsp70 homolog DnaK
Summary for 4B9Q
| Entry DOI | 10.2210/pdb4b9q/pdb |
| Related | 1BPR 1DG4 1DKG 1DKX 1DKY 1DKZ 1Q5L 2BPR |
| Descriptor | CHAPERONE PROTEIN DNAK, ADENOSINE-5'-TRIPHOSPHATE, MAGNESIUM ION, ... (4 entities in total) |
| Functional Keywords | chaperone |
| Biological source | ESCHERICHIA COLI |
| Total number of polymer chains | 4 |
| Total formula weight | 267199.79 |
| Authors | Kopp, J.,Mayer, M.P.,Sinning, I. (deposition date: 2012-09-06, release date: 2012-11-14, Last modification date: 2024-11-06) |
| Primary citation | Kityk, R.,Kopp, J.,Sinning, I.,Mayer, M.P. Structure and Dynamics of the ATP-Bound Open Conformation of Hsp70 Chaperones Mol.Cell, 48:863-, 2012 Cited by PubMed Abstract: Central to the chaperone function of Hsp70s is the transition between open and closed conformations of their polypeptide substrate binding domain (SBD), which is regulated through an allosteric mechanism via ATP binding and hydrolysis in their nucleotide binding domain (NBD). Although the structure of the closed conformation of Hsp70s is well studied, the open conformation has remained elusive. Here, we report on the 2.4 Å crystal structure of the ATP-bound open conformation of the Escherichia coli Hsp70 homolog DnaK. In the open DnaK structure, the β sheet and α-helical lid subdomains of the SBD are detached from one another and docked to different faces of the NBD. The contacts between the β sheet subdomain and the NBD reveal the mechanism of allosteric regulation. In addition, we demonstrate that docking of the β sheet and α-helical lid subdomains to the NBD is a sequential process influenced by peptide and protein substrates. PubMed: 23123194DOI: 10.1016/J.MOLCEL.2012.09.023 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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