{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["7"],"submitter":["Hochmal AK"],"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"],"journal":["Nature communications"],"pagination":["11847"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC4911631"],"repository":["biostudies-literature"],"pubmed_title":["Calredoxin represents a novel type of calcium-dependent sensor-responder connected to redox regulation in the chloroplast."],"pmcid":["PMC4911631"],"pubmed_authors":["Tanaka H","Scholz M","Fufezan C","Hochmal AK","Gabelein P","Mutoh R","Huang K","Finazzi G","Hippler M","Zinzius K","Schulze S","Nordhues A","Petroutsos D","Charoenwattanasatien R","Offenborn JN","Kurisu G","Liu G"],"additional_accession":[]},"is_claimable":false,"name":"Calredoxin represents a novel type of calcium-dependent sensor-responder connected to redox regulation in the chloroplast.","description":"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","dates":{"release":"2016-01-01T00:00:00Z","publication":"2016 Jun","modification":"2026-05-30T06:53:27.877Z","creation":"2019-03-27T02:16:18Z"},"accession":"S-EPMC4911631","cross_references":{"pubmed":["27297041"],"doi":["10.1038/ncomms11847"]}}