4J0B
Structure of mitochondrial Hsp90 (TRAP1) with ADP-BeF3
Summary for 4J0B
| Entry DOI | 10.2210/pdb4j0b/pdb |
| Related | 4IPE 4IVG 4IYN |
| Descriptor | TNF receptor-associated protein 1, COBALT (II) ION, ADENOSINE-5'-DIPHOSPHATE, ... (6 entities in total) |
| Functional Keywords | chaperone, atpase, atp binding, mitochondria, atpase chaperone |
| Biological source | Danio rerio (leopard danio,zebra danio,zebra fish) |
| Total number of polymer chains | 2 |
| Total formula weight | 149280.63 |
| Authors | Partridge, J.R.,Lavery, L.A.,Agard, D.A. (deposition date: 2013-01-30, release date: 2014-01-22, Last modification date: 2024-10-16) |
| Primary citation | Lavery, L.A.,Partridge, J.R.,Ramelot, T.A.,Elnatan, D.,Kennedy, M.A.,Agard, D.A. Structural asymmetry in the closed state of mitochondrial Hsp90 (TRAP1) supports a two-step ATP hydrolysis mechanism. Mol.Cell, 53:330-343, 2014 Cited by PubMed Abstract: While structural symmetry is a prevailing feature of homo-oligomeric proteins, asymmetry provides unique mechanistic opportunities. We present the crystal structure of full-length TRAP1, the mitochondrial Hsp90 molecular chaperone, in a catalytically active closed state. The TRAP1 homodimer adopts a distinct, asymmetric conformation, where one protomer is reconfigured via a helix swap at the middle:C-terminal domain (MD:CTD) interface. This interface plays a critical role in client binding. Solution methods validate the asymmetry and show extension to Hsp90 homologs. Point mutations that disrupt unique contacts at each MD:CTD interface reduce catalytic activity and substrate binding and demonstrate that each protomer needs access to both conformations. Crystallographic data on a dimeric NTD:MD fragment suggests that asymmetry arises from strain induced by simultaneous NTD and CTD dimerization. The observed asymmetry provides the potential for an additional step in the ATPase cycle, allowing sequential ATP hydrolysis steps to drive both client remodeling and client release. PubMed: 24462206DOI: 10.1016/j.molcel.2013.12.023 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.352 Å) |
Structure validation
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