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Crystal structure and functional analysis of human C1ORF123.

Authors :
Rahaman, Siti Nurulnabila A.
Yusop, Jastina Mat
Mohamed-Hussein, Zeti-Azura
Aizat, Wan Mohd
Kok Lian Ho
Aik-Hong Teh
Waterman, Jitka
Boon Keat Tan
Hwei Ling Tan
Li, Adelicia Yongling
Ee Sin Chen
Chyan Leong Ng
Source :
PeerJ; Sep2018, p1-25, 25p
Publication Year :
2018

Abstract

Proteins of the DUF866 superfamily are exclusively found in eukaryotic cells. A member of the DUF866 superfamily, C1ORF123, is a human protein found in the open reading frame 123 of chromosome 1. The physiological role of C1ORF123 is yet to be determined. The only available protein structure of the DUF866 family shares just 26% sequence similarity and does not contain a zinc binding motif. Here, we present the crystal structure of the recombinant human C1ORF123 protein (rC1ORF123). The structure has a 2-fold internal symmetry dividing the monomeric protein into two mirrored halves that comprise of distinct electrostatic potential. The N-terminal half of rC1ORF123 includes a zinc-binding domain interacting with a zinc ion near to a potential ligand binding cavity. Functional studies of human C1ORF123 and its homologue in the fission yeast Schizosaccharomyces pombe (SpEss1) point to a role of DUF866 protein in mitochondrial oxidative phosphorylation. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
21678359
Database :
Complementary Index
Journal :
PeerJ
Publication Type :
Academic Journal
Accession number :
137243349
Full Text :
https://doi.org/10.7717/peerj.5377