4V2L

Crystallographic structure of thioredoxin from Litopenaeus vannamei: Radiation damage effect at 3.4 MGy, focused in disulfide bonds.

4V2L の概要

• エントリーDOI: 10.2210/pdb4v2l/pdb
• 関連するPDBエントリー: 4V2M 4V2N
• 分子名称: THIOREDOXIN, GLYCEROL, SULFATE ION, ... (5 entities in total)
• 機能のキーワード: oxidoreductase, thioredoxin, shrimp, litopenaeus vannamie, radiation damage, disulfide bond
• 由来する生物種: LITOPENAEUS VANNAMEI (PACIFIC WHITE SHRIMP)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 24256.71

構造登録者

Campos-Acevedo, A.A.,Rudino-Pinera, E. (登録日: 2014-10-10, 公開日: 2015-01-14, 最終更新日: 2024-10-16)

主引用文献

Campos-Acevedo, A.A.,Rudino-Pinera, E.
Crystallographic Studies Evidencing the High Energy Tolerance to Disrupting the Interface Disulfide Bond of Thioredoxin 1 from White Leg Shrimp Litopenaeus Vannamei.
Molecules, 19:21113-, 2014

PubMed Abstract: Thioredoxin (Trx) is a small 12-kDa redox protein that catalyzes the reduction of disulfide bonds in proteins from different biological systems. A recent study of the crystal structure of white leg shrimp thioredoxin 1 from Litopenaeus vannamei (LvTrx) revealed a dimeric form of the protein mediated by a covalent link through a disulfide bond between Cys73 from each monomer. In the present study, X-ray-induced damage in the catalytic and the interface disulfide bond of LvTrx was studied at atomic resolution at different transmission energies of 8% and 27%, 12.8 keV at 100 K in the beamline I-24 at Diamond Light Source. We found that at an absorbed dose of 32 MGy, the X-ray induces the cleavage of the disulfide bond of each catalytic site; however, the interface disulfide bond was cleaved at an X-ray adsorbed dose of 85 MGy; despite being the most solvent-exposed disulfide bond in LvTrx (~50 Å2). This result clearly established that the interface disulfide bond is very stable and, therefore, less susceptible to being reduced by X-rays. In fact, these studies open the possibility of the existence in solution of a dimeric LvTrx.

PubMed: 25517346
DOI: 10.3390/MOLECULES191221113

実験手法

X-RAY DIFFRACTION (1.65 Å)