Crystal structure of the bb ' domains of the protein disulfide isomerase ERp57

DOIResolve DOI: http://doi.org/10.1016/j.str.2006.06.019
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TypeArticle
Volume14
Issue8
Pages13311339; # of pages: 9
Subjectcrystal structure; Endoplasmic Reticulum; Enzymes; In Vitro; Mutagenesis; pha; Protein; Proteins; x-ray
AbstractThe 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
Publication date
LanguageEnglish
AffiliationNRC Biotechnology Research Institute; National Research Council Canada
Note200639
Peer reviewedNo
NRC number47534
NPARC number3539705
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Record identifierc5649607-0471-43ac-8b03-0f70e8df6cd7
Record created2009-03-01
Record modified2016-05-09
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