5ZLQ

Crystal Structure of C1orf123

5ZLQ の概要

• エントリーDOI: 10.2210/pdb5zlq/pdb
• 分子名称: UPF0587 protein C1orf123, ZINC ION (3 entities in total)
• 機能のキーワード: zn-containing, cys-x-x-cys motif, metal binding protein
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 18288.00

構造登録者

Furukawa, Y.,Lim, C.T.,Tosha, T. (登録日: 2018-03-29, 公開日: 2018-10-10, 最終更新日: 2024-03-27)

主引用文献

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

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: 30260988
DOI: 10.1371/journal.pone.0204355

実験手法

X-RAY DIFFRACTION (2 Å)