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5E37

Redox protein from Chlamydomonas reinhardtii

Summary for 5E37
Entry DOI10.2210/pdb5e37/pdb
DescriptorEF-Hand domain-containing thioredoxin, CALCIUM ION (3 entities in total)
Functional Keywordscalredoxin, calcium-, redox-, chlamydomonas reinhardtii, oxidoreductase
Biological sourceChlamydomonas reinhardtii
Total number of polymer chains2
Total formula weight80221.42
Authors
Charoenwattansatien, R.,Hochmal, A.K.,Zinzius, K.,Muto, R.,Tanaka, H.,Hippler, M.,Kurisu, G. (deposition date: 2015-10-02, release date: 2016-06-22, Last modification date: 2024-10-23)
Primary citationHochmal, A.K.,Zinzius, K.,Charoenwattanasatien, R.,Gabelein, P.,Mutoh, R.,Tanaka, H.,Schulze, S.,Liu, G.,Scholz, M.,Nordhues, A.,Offenborn, J.N.,Petroutsos, D.,Finazzi, G.,Fufezan, C.,Huang, K.,Kurisu, G.,Hippler, M.
Calredoxin represents a novel type of calcium-dependent sensor-responder connected to redox regulation in the chloroplast
Nat Commun, 7:11847-11847, 2016
Cited by
PubMed Abstract: Calcium (Ca(2+)) and redox signalling play important roles in acclimation processes from archaea to eukaryotic organisms. Herein we characterized a unique protein from Chlamydomonas reinhardtii that has the competence to integrate Ca(2+)- and redox-related signalling. This protein, designated as calredoxin (CRX), combines four Ca(2+)-binding EF-hands and a thioredoxin (TRX) domain. A crystal structure of CRX, at 1.6 Å resolution, revealed an unusual calmodulin-fold of the Ca(2+)-binding EF-hands, which is functionally linked via an inter-domain communication path with the enzymatically active TRX domain. CRX is chloroplast-localized and interacted with a chloroplast 2-Cys peroxiredoxin (PRX1). Ca(2+)-binding to CRX is critical for its TRX activity and for efficient binding and reduction of PRX1. Thereby, CRX represents a new class of Ca(2+)-dependent 'sensor-responder' proteins. Genetically engineered Chlamydomonas strains with strongly diminished amounts of CRX revealed altered photosynthetic electron transfer and were affected in oxidative stress response underpinning a function of CRX in stress acclimation.
PubMed: 27297041
DOI: 10.1038/ncomms11847
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.6 Å)
Structure validation

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数据于2024-10-30公开中

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