4iyn | pdb_00004iyn

Structure of mitochondrial Hsp90 (TRAP1) with ADP-ALF4-

spinqualitylabelsall models 4iyn, resolution 2.31Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4iyn is a 2 chain structure with sequence from Danio rerio. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.312Å Ligands: ADP, ALF, CO, MG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A8WFV1_DANRE Publication Abstract from PubMed 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. Structural asymmetry in the closed state of mitochondrial Hsp90 (TRAP1) supports a two-step ATP hydrolysis mechanism.,Lavery LA, Partridge JR, Ramelot TA, Elnatan D, Kennedy MA, Agard DA Mol Cell. 2014 Jan 23;53(2):330-43. doi: 10.1016/j.molcel.2013.12.023. PMID:24462206 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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