Loading
PDBj
メニューPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

5FIG

APO-CSP3 (COPPER STORAGE PROTEIN 3) FROM BACILLUS SUBTILIS

5FIG の概要
エントリーDOI10.2210/pdb5fig/pdb
関連するPDBエントリー5ARM 5ARN
分子名称CSP3 (2 entities in total)
機能のキーワードcopper-binding protein, copper storage, bacillus subtilis
由来する生物種BACILLUS SUBTILIS
タンパク質・核酸の鎖数6
化学式量合計71122.55
構造登録者
Vita, N.,Landolfi, G.,Basle, A.,Platsaki, S.,Waldron, K.,Dennison, C. (登録日: 2015-09-25, 公開日: 2016-10-12, 最終更新日: 2024-01-10)
主引用文献Vita, N.,Landolfi, G.,Basle, A.,Platsaki, S.,Lee, J.,Waldron, K.J.,Dennison, C.
Bacterial cytosolic proteins with a high capacity for Cu(I) that protect against copper toxicity.
Sci Rep, 6:39065-39065, 2016
Cited by
PubMed Abstract: Bacteria are thought to avoid using the essential metal ion copper in their cytosol due to its toxicity. Herein we characterize Csp3, the cytosolic member of a new family of bacterial copper storage proteins from Methylosinus trichosporium OB3b and Bacillus subtilis. These tetrameric proteins possess a large number of Cys residues that point into the cores of their four-helix bundle monomers. The Csp3 tetramers can bind a maximum of approximately 80 Cu(I) ions, mainly via thiolate groups, with average affinities in the (1-2) × 10 M range. Cu(I) removal from these Csp3s by higher affinity potential physiological partners and small-molecule ligands is very slow, which is unexpected for a metal-storage protein. In vivo data demonstrate that Csp3s prevent toxicity caused by the presence of excess copper. Furthermore, bacteria expressing Csp3 accumulate copper and are able to safely maintain large quantities of this metal ion in their cytosol. This suggests a requirement for storing copper in this compartment of Csp3-producing bacteria.
PubMed: 27991525
DOI: 10.1038/srep39065
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.7 Å)
構造検証レポート
Validation report summary of 5fig
検証レポート(詳細版)ダウンロードをダウンロード

226707

件を2024-10-30に公開中

PDB statisticsPDBj update infoContact PDBjnumon