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Crystal structure and functional analysis of human C1ORF123


Citation

A. Rahaman, Siti Nurulnabila and Mat Yusop, Jastina and Mohamed Hussein, Zeti Azura and Wan Kamaruddin, Wan Mohd Aizat and Ho, Kok Lian and Teh, Aik Hong and Waterman, Jitka and Tan, Boon Keat and Tan, Hwei Ling and Li, Adelicia Yongling and Chen, Ee Sin and Ng, Chyan Leong (2018) Crystal structure and functional analysis of human C1ORF123. PeerJ, 6. pp. 1-25. ISSN 2167-8359

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.


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Additional Metadata

Item Type: Article
Divisions: Faculty of Medicine and Health Science
DOI Number: https://doi.org/10.7717/peerj.5377
Publisher: PeerJ
Keywords: C1ORF123; DUF866; Internal symmetry; Zinc-binding domain; Mitochondrial oxidative phosphorylation; Crystal structure; CXXC motif
Depositing User: Nurul Ainie Mokhtar
Date Deposited: 04 Mar 2020 07:45
Last Modified: 04 Mar 2020 07:45
Altmetrics: http://www.altmetric.com/details.php?domain=psasir.upm.edu.my&doi=10.7717/peerj.5377
URI: http://psasir.upm.edu.my/id/eprint/72149
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