2BJX

PROTEIN DISULFIDE ISOMERASE

2BJX の概要

• エントリーDOI: 10.2210/pdb2bjx/pdb
• 分子名称: PROTEIN (PROTEIN DISULFIDE ISOMERASE) (1 entity in total)
• 機能のキーワード: electron transport, redox-active center, isomerase, endoplasmic reticulum
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 12072.30

構造登録者

Kemmink, J.,Dijkstra, K.,Mariani, M.,Scheek, R.M.,Penka, E.,Nilges, M.,Darby, N.J. (登録日: 1999-01-30, 公開日: 1999-02-09, 最終更新日: 2023-12-27)

主引用文献

Kemmink, J.,Dijkstra, K.,Mariani, M.,Scheek, R.M.,Penka, E.,Nilges, M.,Darby, N.J.
The structure in solution of the b domain of protein disulfide isomerase.
J.Biomol.NMR, 13:357-368, 1999

PubMed Abstract: Protein disulfide isomerase (PDI) is a multifunctional protein of the endoplasmic reticulum, which catalyzes the formation, breakage and rearrangement of disulfide bonds during protein folding. It consists of four domains designated a, b, b and a. Both a and a domains contains an active site with the sequence motif -Cys-Gly-His-Cys-involved directly in thiol-disulfide exchange reactions. As expected these domains have structures very similar to the ubiquitous redox protein thioredoxin. A low-resolution NMR structure of the b domain revealed that this domain adopts a fold similar to the PDI a domain and thioredoxin [Kemmink, J., Darby, N.J., Dijkstra, K., Nilges, M. and Creighton, T.E. (1997) Curr. Biol. 7, 239-245]. A refined ensemble of solution structures based on the input of 1865 structural restraints shows that the structure of PDI b is well defined throughout the complete protein except for about 10 residues at the C-terminus of the sequence. 15N relaxation data show that these residues are disordered and not part of this structural domain. Therefore the domain boundaries of PDI can now be fixed with reasonable precision. Structural comparison of the PDI b domain with thioredoxin and PDI a reveals several features important for thiol-disulfide exchange activity.

PubMed: 10383197
DOI: 10.1023/A:1008341820489

実験手法

SOLUTION NMR