2H8L

Crystal structure of the bb' fragment of ERp57

2H8L の概要

• エントリーDOI: 10.2210/pdb2h8l/pdb
• 分子名称: Protein disulfide-isomerase A3 (2 entities in total)
• 機能のキーワード: thioredoxin-like fold, isomerase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Endoplasmic reticulum lumen (By similarity): P30101
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 86455.47

構造登録者

Kozlov, G.,Schrag, J.D.,Cygler, M.,Gehring, K. (登録日: 2006-06-07, 公開日: 2006-08-29, 最終更新日: 2024-11-13)

主引用文献

Kozlov, G.,Maattanen, P.,Schrag, J.D.,Pollock, S.,Cygler, M.,Nagar, B.,Thomas, D.Y.,Gehring, K.
Crystal Structure of the bb' Domains of the Protein Disulfide Isomerase ERp57.
Structure, 14:1331-1339, 2006

PubMed Abstract: 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.

PubMed: 16905107
DOI: 10.1016/j.str.2006.06.019

実験手法

X-RAY DIFFRACTION (2 Å)