2h8l
From Proteopedia
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Crystal structure of the bb' fragment of ERp57
Overview
The synthesis of proteins in the endoplasmic reticulum (ER) is limited by, the rate of correct disulfide bond formation. This process is carried out, by protein disulfide isomerases, a family of ER proteins which includes, general enzymes such as PDI that recognize unfolded proteins and others, that are selective for specific proteins or classes. Using small-angle, X-ray scattering and X-ray crystallography, we report the structure of a, selective isomerase, ERp57, and its interactions with the lectin chaperone, calnexin. Using isothermal titration calorimetry and NMR spectroscopy, we, show that the b' domain of ERp57 binds calnexin with micromolar affinity, through a conserved patch of basic residues. Disruption of this binding, site by mutagenesis abrogates folding of RNase B in an in vitro assay. The, relative positions of the ERp57 catalytic sites and calnexin binding site, suggest that activation by calnexin is due to substrate recruitment rather, than a direct stimulation of ERp57 oxidoreductase activity.
About this Structure
2H8L is a Single protein structure of sequence from Homo sapiens. Active as Protein disulfide-isomerase, with EC number 5.3.4.1 Full crystallographic information is available from OCA.
Reference
Crystal structure of the bb' domains of the protein disulfide isomerase ERp57., Kozlov G, Maattanen P, Schrag JD, Pollock S, Cygler M, Nagar B, Thomas DY, Gehring K, Structure. 2006 Aug;14(8):1331-9. PMID:16905107
Page seeded by OCA on Fri Feb 15 17:30:26 2008
