Please use this identifier to cite or link to this item: https://doi.org/10.7717/peerj.5377
Title: Crystal structure and functional analysis of human C1ORF123
Authors: Rahaman, S.N.A
Yusop, J.M
Mohamed-Hussein, Z.-A
Aizat, W.M
Ho, K.L
Teh, A.-H
Waterman, J
Tan, B.K
Tan, H.L 
Li, A.Y 
Chen, E.S 
Ng, C.L
Issue Date: 2018
Citation: Rahaman, S.N.A, Yusop, J.M, Mohamed-Hussein, Z.-A, Aizat, W.M, Ho, K.L, Teh, A.-H, Waterman, J, Tan, B.K, Tan, H.L, Li, A.Y, Chen, E.S, Ng, C.L (2018). Crystal structure and functional analysis of human C1ORF123. PeerJ 2018 (9) : e5377. ScholarBank@NUS Repository. https://doi.org/10.7717/peerj.5377
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. Copyright 2018 A. Rahaman et al.
Source Title: PeerJ
URI: https://scholarbank.nus.edu.sg/handle/10635/176062
ISSN: 2167-8359
DOI: 10.7717/peerj.5377
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