1WOU

Crystal Structure of human Trp14

Summary for 1WOU

• Entry DOI: 10.2210/pdb1wou/pdb
• Descriptor: thioredoxin -related protein, 14 kDa (1 entity in total)
• Functional Keywords: electron transport
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm: Q9BRA2
• Total number of polymer chains: 1
• Total formula weight: 13957.79

Authors

Woo, J.R.,Kim, S.J.,Jeong, W.,Cho, Y.H.,Lee, S.C.,Chung, Y.J.,Rhee, S.G.,Ryu, S.E. (deposition date: 2004-08-25, release date: 2004-09-14, Last modification date: 2024-10-23)

Primary citation

Woo, J.R.,Kim, S.J.,Jeong, W.,Cho, Y.H.,Lee, S.C.,Chung, Y.J.,Rhee, S.G.,Ryu, S.E.
Structural basis of cellular redox regulation by human TRP14
J.Biol.Chem., 279:48120-48125, 2004

PubMed Abstract: Thioredoxin-related protein 14 (TRP14) is involved in regulating tumor necrosis factor-alpha-induced signaling pathways in a different manner from human thioredoxin 1 (Trx1). Here, we report the crystal structure of human TRP14 determined at 1.8-A resolutions. The structure reveals a typical thioredoxin fold with characteristic structural features that account for the substrate specificity of the protein. The surface of TRP14 in the vicinity of the active site includes an extended loop and an additional alpha-helix, and the distribution of charged residues in the surface is different from Trx1. The distinctive dipeptide between the redox-active cysteines contributes to stabilizing the thiolate anion of the active site cysteine 43, increasing reactivity of the cysteine toward substrates. These structural differences in the active site suggest that TRP14 has evolved to regulate cellular redox signaling by recognizing a distinctive group of substrates that would complement the group of proteins regulated by Trx1.

PubMed: 15355959
DOI: 10.1074/jbc.M407079200

Experimental method

X-RAY DIFFRACTION (1.8 Å)