1TBW
Ligand Induced Conformational Shift in the N-terminal Domain of GRP94, Open Conformation
Summary for 1TBW
| Entry DOI | 10.2210/pdb1tbw/pdb |
| Related | 1QY5 1QY8 1QYE 1QYH 1TC0 1TC6 |
| Descriptor | Endoplasmin, MAGNESIUM ION, ADENOSINE MONOPHOSPHATE, ... (5 entities in total) |
| Functional Keywords | grp94, hsp90, amp, bergrat, chaperone, endoplasmic reticulum |
| Biological source | Canis lupus familiaris (dog) More |
| Cellular location | Endoplasmic reticulum lumen: P41148 |
| Total number of polymer chains | 2 |
| Total formula weight | 54742.21 |
| Authors | Gewirth, D.T.,Immormino, R.M.,Dollins, D.E.,Shaffer, P.L.,Walker, M.A.,Soldano, K.L. (deposition date: 2004-05-20, release date: 2004-08-24, Last modification date: 2024-02-14) |
| Primary citation | Immormino, R.M.,Dollins, D.E.,Shaffer, P.L.,Soldano, K.L.,Walker, M.A.,Gewirth, D.T. Ligand-induced Conformational Shift in the N-terminal Domain of GRP94, an Hsp90 Chaperone. J.Biol.Chem., 279:46162-46171, 2004 Cited by PubMed Abstract: 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. PubMed: 15292259DOI: 10.1074/jbc.M405253200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.15 Å) |
Structure validation
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