6J13

Redox protein from Chlamydomonas reinhardtii

Summary for 6J13

• Entry DOI: 10.2210/pdb6j13/pdb
• Descriptor: 2-cys peroxiredoxin (2 entities in total)
• Functional Keywords: peroxiredoxin, redox-, chlamydomonas reinhardtii, oxidoreductase
• Biological source: Chlamydomonas reinhardtii (Chlamydomonas smithii)
• Total number of polymer chains: 10
• Total formula weight: 246927.83

Authors

Charoenwattansatien, R.,Zinzius, K.,Tanaka, H.,Hippler, M.,Kurisu, G. (deposition date: 2018-12-27, release date: 2019-12-04, Last modification date: 2023-11-22)

Primary citation

Charoenwattanasatien, R.,Zinzius, K.,Scholz, M.,Wicke, S.,Tanaka, H.,Brandenburg, J.S.,Marchetti, G.M.,Ikegami, T.,Matsumoto, T.,Oda, T.,Sato, M.,Hippler, M.,Kurisu, G.
Calcium sensing via EF-hand 4 enables thioredoxin activity in the sensor-responder protein calredoxin in the green algaChlamydomonas reinhardtii.
J.Biol.Chem., 295:170-180, 2020

PubMed Abstract: Calcium (Ca) and redox signaling enable cells to quickly adapt to changing environments. The signaling protein calredoxin (CRX) from the green alga is a chloroplast-resident thioredoxin having Ca-dependent activity and harboring a unique combination of an EF-hand domain connected to a typical thioredoxin-fold. Using small-angle X-ray scattering (SAXS), FRET, and NMR techniques, we found that Ca-binding not only induces a conformational change in the EF-hand domain, but also in the thioredoxin domain, translating into the onset of thioredoxin redox activity. Functional analyses of CRX with genetically altered EF-hands revealed that EF-hand 4 is important for mediating the communication between the two domains. Moreover, we crystallized a variant (C174S) of the CRX target protein peroxiredoxin 1 (PRX1) at 2.4 Å resolution, modeled the interaction complex of the two proteins, and analyzed it by cross-linking and MS analyses, revealing that the interaction interface is located close to the active sites of both proteins. Our findings shed light on the Ca binding-induced changes in CRX structure in solution at the level of the overall protein and individual domains and residues.

PubMed: 31776187
DOI: 10.1074/jbc.RA119.008735

Experimental method

X-RAY DIFFRACTION (2.4 Å)