1U2O

Crystal Structure Of The N-Domain Of Grp94 Lacking The Charged Domain In Complex With Neca

Replaces:  1QYH

Summary for 1U2O

• Entry DOI: 10.2210/pdb1u2o/pdb
• Related: 1QY5 1QY8 1QYE
• Descriptor: Endoplasmin, N-ETHYL-5'-CARBOXAMIDO ADENOSINE, TETRAETHYLENE GLYCOL, ... (5 entities in total)
• Functional Keywords: grp94, hsp90, bergerat, chaperone, endoplasmic reticulum, neca
• Biological source: Canis lupus familiaris (dog); More
• Cellular location: Endoplasmic reticulum lumen: P41148
• Total number of polymer chains: 2
• Total formula weight: 54854.02

Authors

Soldano, K.L.,Jivan, A.,Nicchitta, C.V.,Gewirth, D.T. (deposition date: 2004-07-19, release date: 2004-08-03, Last modification date: 2023-10-25)

Primary citation

Soldano, K.L.,Jivan, A.,Nicchitta, C.V.,Gewirth, D.T.
Structure of the N-terminal domain of GRP94. Basis for ligand specificity and regulation
J.Biol.Chem., 278:48330-48338, 2003

PubMed Abstract: GRP94, the endoplasmic reticulum (ER) paralog of the chaperone Hsp90, plays an essential role in the structural maturation or secretion of a subset of proteins destined for transport to the cell surface, such as the Toll-like receptors 2 and 4, and IgG, respectively. GRP94 differs from cytoplasmic Hsp90 by exhibiting very weak ATP binding and hydrolysis activity. GRP94 also binds selectively to a series of substituted adenosine analogs. The high resolution crystal structures at 1.75-2.1 A of the N-terminal and adjacent charged domains of GRP94 in complex with N-ethylcarboxamidoadenosine, radicicol, and 2-chlorodideoxyadenosine reveals a structural mechanism for ligand discrimination among hsp90 family members. The structures also identify a putative subdomain that may act as a ligand-responsive switch. The residues of the charged region fold into a disordered loop whose termini are ordered and continue the twisted beta sheet that forms the structural core of the N-domain. This continuation of the beta sheet past the charged domain suggests a structural basis for the association of the N-terminal and middle domains of the full-length chaperone.

PubMed: 12970348
DOI: 10.1074/jbc.M308661200

Experimental method

X-RAY DIFFRACTION (2.1 Å)