1tc6 | pdb_00001tc6

Ligand Induced Conformational Shift in the N-terminal Domain of GRP94, Open Conformation ADP-Complex

spinqualitylabelsall models 1tc6, resolution 1.87Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1tc6 is a 2 chain structure with sequence from Canfa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ADP, MG, PG4 Related: 1qy5, 1qy8, 1qye, 1qyh, 1tbw, 1tc0 Gene: TRA1 (CANFA) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [ENPL_CANFA] Molecular chaperone that functions in the processing and transport of secreted proteins. When associated with CNPY3, required for proper folding of Toll-like receptors. Functions in endoplasmic reticulum associated degradation (ERAD). Has ATPase activity (By similarity). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Heat Shock Protein structures

Proteopedia Page Contributors and Editors (what is this?)

OCA