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Arabidopsis thaliana Hcc1 is a Sco‐like metallochaperone for Cu A assembly in Cytochrome c Oxidase
Author(s) -
Llases MaríaEugenia,
Lisa MaríaNatalia,
Morgada Marcos N.,
Giannini Estefanía,
Alzari Pedro M.,
Vila Alejandro J.
Publication year - 2020
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/febs.15016
Subject(s) - arabidopsis thaliana , arabidopsis , cytochrome c oxidase , protein data bank (rcsb pdb) , thermostability , biochemistry , chemistry , oxidoreductase , molecular replacement , biology , protein structure , gene , enzyme , mutant
The assembly of the Cu A site in Cytochrome c Oxidase ( COX ) is a critical step for aerobic respiration in COX ‐dependent organisms. Several gene products have been associated with the assembly of this copper site, the most conserved of them belonging to the Sco family of proteins, which have been shown to perform different roles in different organisms. Plants express two orthologs of Sco proteins: Hcc1 and Hcc2. Hcc1 is known to be essential for plant development and for COX maturation, but its precise function has not been addressed until now. Here, we report the biochemical, structural and functional characterization of Arabidopsis thaliana Hcc1 protein (here renamed Sco1). We solved the crystal structure of the Cu +1 ‐bound soluble domain of this protein, revealing a tri coordinated environment involving a CxxxCx n H motif. We show that At Sco1 is able to work as a copper metallochaperone, inserting two Cu +1 ions into the Cu A site in a model of Cox II . We also show that At Sco1 does not act as a thiol‐disulfide oxido‐reductase. Overall, this information sheds new light on the biochemistry of Sco proteins, highlighting the diversity of functions among them despite their high structural similarities. Database PDB entry 6N5U (Crystal structure of Arabidopsis thaliana ScoI with copper bound).