2IPA

solution structure of Trx-ArsC complex

Summary for 2IPA

• Entry DOI: 10.2210/pdb2ipa/pdb
• NMR Information: BMRB: 15028
• Descriptor: Thioredoxin, Protein arsC (2 entities in total)
• Functional Keywords: solution structure, complex, electron transport-oxidoreductase complex, electron transport/oxidoreductase
• Biological source: Bacillus subtilis; More
• Total number of polymer chains: 2
• Total formula weight: 26938.35

Authors

Jin, C.,Hu, Y.,Li, Y.,Zhang, X. (deposition date: 2006-10-12, release date: 2007-02-13, Last modification date: 2021-11-10)

Primary citation

Li, Y.,Hu, Y.,Zhang, X.,Xu, H.,Lescop, E.,Xia, B.,Jin, C.
Conformational fluctuations coupled to the thiol-disulfide transfer between thioredoxin and arsenate reductase in Bacillus subtilis.
J.Biol.Chem., 282:11078-11083, 2007

PubMed Abstract: Arsenic compounds commonly exist in nature and are toxic to nearly all kinds of life forms, which directed the evolution of enzymes in many organisms for arsenic detoxification. In bacteria, the thioredoxin-coupled arsenate reductase catalyzes the reduction of arsenate to arsenite by intramolecular thiol-disulfide cascade. The oxidized arsenate reductase ArsC is subsequently regenerated by thioredoxin through an intermolecular thiol-disulfide exchange process. The solution structure of the Bacillus subtilis thioredoxin-arsenate reductase complex represents the transiently formed intermediate during the intermolecular thiol-disulfide exchange reaction. A comparison of the complex structure with that of thioredoxin and arsenate reductase proteins in redox states showed substantial conformational changes coupled to the reaction process, with arsenate reductase, especially, adopting an "intermediate" conformation in the complex. Our current studies provide novel insights into understanding the reaction mechanisms of the thioredoxin-arsenate reductase pathway.

PubMed: 17303556
DOI: 10.1074/jbc.M700970200

Experimental method

SOLUTION NMR