5ZLQ
Crystal Structure of C1orf123
Summary for 5ZLQ
| Entry DOI | 10.2210/pdb5zlq/pdb |
| Descriptor | UPF0587 protein C1orf123, ZINC ION (3 entities in total) |
| Functional Keywords | zn-containing, cys-x-x-cys motif, metal binding protein |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 1 |
| Total formula weight | 18288.00 |
| Authors | Furukawa, Y.,Lim, C.T.,Tosha, T. (deposition date: 2018-03-29, release date: 2018-10-10, Last modification date: 2024-03-27) |
| Primary citation | Furukawa, Y.,Lim, C.,Tosha, T.,Yoshida, K.,Hagai, T.,Akiyama, S.,Watanabe, S.,Nakagome, K.,Shiro, Y. Identification of a novel zinc-binding protein, C1orf123, as an interactor with a heavy metal-associated domain PLoS ONE, 13:e0204355-e0204355, 2018 Cited by PubMed Abstract: Heavy metal-associated (HMA) domains bind metal ions at its Cys-x-x-Cys (CxxC) motif and constitute an intracellular network for trafficking of metal ions for utilization and detoxification. We thus expect that novel metalloproteins can be identified by screening proteins interacting with a HMA domain. In this study, we performed yeast two-hybrid screening of the human proteome and found an uncharacterized protein encoded as open reading frame 123 in chromosome 1 (C1orf123) that can interact specifically with the HMA domain of a copper chaperone for superoxide dismutase (CCSdI). Our X-ray structural analysis of C1orf123 further revealed that it binds a Zn2+ ion in a tetrahedral coordination with four thiolate groups from two conserved CxxC motifs. For the interaction between C1orf123 and CCSdI, the CxxC motifs in both C1orf123 and CCSdI were required, implying metal-mediated interaction through the CxxC motifs. Notably, C1orf123 did not interact with several other HMA domains containing CxxC motifs, supporting high specificity in the interaction between C1orf123 and CCSdI. Based upon these results, we further discuss functional and structural significance of the interaction between C1orf123 and CCS. PubMed: 30260988DOI: 10.1371/journal.pone.0204355 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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