Crystal structure and functional analysis of human C1ORF123

DOI: 10.7717/peerj.5377

Authors: Siti Nurulnabila A. Rahaman (Universiti Kebangsaan Malaysia) , Jastina Mat Yusop (Universiti Kebangsaan Malaysia) , Zeti-Azura Mohamed-Hussein (Universiti Kebangsaan Malaysia) , Wan Mohd Aizat (Universiti Kebangsaan Malaysia) , Kok Lian Ho (Universiti Kebangsaan Malaysia) , Aik-Hong Teh (Universiti Sains Malaysia) , Jitka Waterman (Diamond Light Source) , Boon Keat Tan (International Medical University) , Hwei Ling Tan (National University of Singapore) , Adelicia Yongling Li (National University of Singapore) , Ee Sin Chen (National University of Singapore) , Chyan Leong Ng (Universiti Kebangsaan Malaysia)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Peerj , VOL 6

State: Published (Approved)
Published: September 2018
Diamond Proposal Number(s): 5073 , 11651

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.

Journal Keywords: C1ORF123; DUF866; Internal symmetry; Zinc-binding domain; Mitochondrial oxidative phosphorylation; Crystal structure; CXXC motif

Subject Areas: Biology and Bio-materials, Chemistry


Instruments: I02-Macromolecular Crystallography , I04-Macromolecular Crystallography

Added On: 10/10/2018 09:04

Discipline Tags:

Biochemistry Chemistry Structural biology Biophysics Life Sciences & Biotech

Technical Tags:

Diffraction Macromolecular Crystallography (MX)