3DYR

Crystal structure of E. coli thioredoxin mutant I76T in its oxidized form

3DYR の概要

• エントリーDOI: 10.2210/pdb3dyr/pdb
• 分子名称: Thioredoxin-1 (2 entities in total)
• 機能のキーワード: mutant protein, electron transport, host-virus interaction, redox-active center, transport
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 23749.08

構造登録者

Ren, G.,Bardwell, J.C.A.,Xu, Z. (登録日: 2008-07-28, 公開日: 2009-01-27, 最終更新日: 2024-10-09)

主引用文献

Ren, G.,Stephan, D.,Xu, Z.,Zheng, Y.,Tang, D.,Harrison, R.S.,Kurz, M.,Jarrott, R.,Shouldice, S.R.,Hiniker, A.,Martin, J.L.,Heras, B.,Bardwell, J.C.
Properties of the thioredoxin fold superfamily are modulated by a single amino acid residue.
J.Biol.Chem., 284:10150-10159, 2009

PubMed Abstract: The ubiquitous thioredoxin fold proteins catalyze oxidation, reduction, or disulfide exchange reactions depending on their redox properties. They also play vital roles in protein folding, redox control, and disease. Here, we have shown that a single residue strongly modifies both the redox properties of thioredoxin fold proteins and their ability to interact with substrates. This residue is adjacent in three-dimensional space to the characteristic CXXC active site motif of thioredoxin fold proteins but distant in sequence. This residue is just N-terminal to the conservative cis-proline. It is isoleucine 75 in the case of thioredoxin. Our findings support the conclusion that a very small percentage of the amino acid residues of thioredoxin-related proteins are capable of dictating the functions of these proteins.

PubMed: 19181668
DOI: 10.1074/jbc.M809509200

実験手法

X-RAY DIFFRACTION (2 Å)