7ME6

Structure of the apo form of YcnI

7ME6 の概要

• エントリーDOI: 10.2210/pdb7me6/pdb
• 分子名称: Uncharacterized protein YcnI, MALONATE ION (3 entities in total)
• 機能のキーワード: cupredoxin, cu-binding, metal binding protein
• 由来する生物種: Bacillus subtilis
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 29091.67

構造登録者

Damle, M.,Fisher, O.S. (登録日: 2021-04-06, 公開日: 2021-08-18, 最終更新日: 2024-04-03)

主引用文献

Damle, M.S.,Singh, A.N.,Peters, S.C.,Szalai, V.A.,Fisher, O.S.
The YcnI protein from Bacillus subtilis contains a copper-binding domain.
J.Biol.Chem., 297:101078-101078, 2021

PubMed Abstract: Bacteria require a precise balance of copper ions to ensure that essential cuproproteins are fully metalated while also avoiding copper-induced toxicity. The Gram-positive bacterium Bacillus subtilis maintains appropriate copper homeostasis in part through the ycn operon. The ycn operon comprises genes encoding three proteins: the putative copper importer YcnJ, the copper-dependent transcriptional repressor YcnK, and the uncharacterized Domain of Unknown Function 1775 (DUF1775) containing YcnI. DUF1775 domains are found across bacterial phylogeny, and bioinformatics analyses indicate that they frequently neighbor domains implicated in copper homeostasis and transport. Here, we investigated whether YcnI can interact with copper and, using electron paramagnetic resonance and inductively coupled plasma-MS, found that this protein can bind a single Cu(II) ion. We determine the structure of both the apo and copper-bound forms of the protein by X-ray crystallography, uncovering a copper-binding site featuring a unique monohistidine brace ligand set that is highly conserved among DUF1775 domains. These data suggest a possible role for YcnI as a copper chaperone and that DUF1775 domains in other bacterial species may also function in copper homeostasis.

PubMed: 34400169
DOI: 10.1016/j.jbc.2021.101078

実験手法

X-RAY DIFFRACTION (2.053 Å)