5DQY

A fully oxidized human thioredoxin

Summary for 5DQY

• Entry DOI: 10.2210/pdb5dqy/pdb
• Descriptor: Thioredoxin, BENZOIC ACID, CHLORIDE ION, ... (5 entities in total)
• Functional Keywords: oxidoreductase
• Biological source: Homo sapiens (Human)
• Cellular location: Nucleus: P10599
• Total number of polymer chains: 1
• Total formula weight: 12000.15

Authors

Hwang, J. (deposition date: 2015-09-15, release date: 2015-12-23)

Primary citation

Hwang, J.,Nguyen, L.T.,Jeon, Y.H.,Lee, C.Y.,Kim, M.H.
Crystal structure of fully oxidized human thioredoxin.
Biochem.Biophys.Res.Commun., 467:218-222, 2015

PubMed Abstract: In addition to the active cysteines located at positions 32 and 35 in humans, mammalian cytosolic thioredoxin (TRX) possesses additional conserved cysteine residues at positions 62, 69, and 73. These non-canonical cysteine residues, that are distinct from prokaryotic TRX and also not found in mammalian mitochondrial TRX, have been implicated in biological functions regulating signal transduction pathways via their post-translational modifications. Here, we describe for the first time the structure of a fully oxidized TRX. The structure shows a non-active Cys62-Cys69 disulfide bond in addition to the active Cys32-Cys35 disulfide. The non-active disulfide switches the α3-helix of TRX, composed of residues Cys62 to Glu70, to a bulging loop and dramatically changes the environment of the TRX residues involved in the interaction with its reductase and other cellular substrates. This structural modification may have implications for a number of potential functions of TRX including the regulation of redox-dependent signaling pathways.

PubMed: 26453009
DOI: 10.1016/j.bbrc.2015.10.003

Experimental method

X-RAY DIFFRACTION (1.4 Å)