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spinqualitylabelsall models 1tc0, resolution 2.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Ligand Induced Conformational Shifts in the N-terminal Domain of GRP94, Open Conformation Complexed with the physiological partner ATP

Overview

GRP94 is the endoplasmic reticulum paralog of cytoplasmic Hsp90. Models of, Hsp90 action posit an ATP-dependent conformational switch in the, N-terminal ligand regulatory domain of the chaperone. However, crystal, structures of the isolated N-domain of Hsp90 in complex with a variety of, ligands have yet to demonstrate such a conformational change. We have, determined the structure of the N-domain of GRP94 in complex with ATP, ADP, and AMP. Compared with the N-ethylcarboxamidoadenosine and, radicicol-bound forms, these structures reveal a large conformational, rearrangement in the protein. The nucleotide-bound form exposes new, surfaces that interact to form a biochemically plausible dimer that is, reminiscent of those seen in structures of MutL and DNA gyrase. Weak ATP, binding and a conformational change in response to ligand identity are, distinctive mechanistic features of GRP94 and suggest a model for how, GRP94 functions in the absence of co-chaperones and ATP hydrolysis.

About this Structure

1TC0 is a Single protein structure of sequence from Canis lupus familiaris with MG, ATP and PG4 as ligands. Full crystallographic information is available from OCA.

Reference

Ligand-induced conformational shift in the N-terminal domain of GRP94, an Hsp90 chaperone., Immormino RM, Dollins DE, Shaffer PL, Soldano KL, Walker MA, Gewirth DT, J Biol Chem. 2004 Oct 29;279(44):46162-71. Epub 2004 Aug 2. PMID:15292259

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