7PJO

Crystal form 3 of CPR-C4: a cysteine protease from the Candidate Phyla Radiation

これはPDB形式変換不可エントリーです。

7PJO の概要

• エントリーDOI: 10.2210/pdb7pjo/pdb
• 関連するPDBエントリー: 7OB6 7OB7
• 分子名称: CPR-C4, PHOSPHATE ION (3 entities in total)
• 機能のキーワード: cysteine protease, hydrolase
• 由来する生物種: Candidate division CPR1
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 55042.87

構造登録者

Cornish, K.A.S.,Pohl, E. (登録日: 2021-08-24, 公開日: 2022-07-06, 最終更新日: 2024-01-31)

主引用文献

Cornish, K.A.S.,Lange, J.,Aevarsson, A.,Pohl, E.
CPR-C4 is a highly conserved novel protease from the Candidate Phyla Radiation with remote structural homology to human vasohibins.
J.Biol.Chem., 298:101919-101919, 2022

PubMed Abstract: The Candidate Phyla Radiation is a recently uncovered and vast expansion of the bacterial domain of life, made up of largely uncharacterized phyla that lack isolated representatives. This unexplored territory of genetic diversity presents an abundance of novel proteins with potential applications in the life-science sectors. Here, we present the structural and functional elucidation of CPR-C4, a hypothetical protein from the genome of a thermophilic Candidate Phyla Radiation organism, identified through metagenomic sequencing. Our analyses revealed that CPR-C4 is a member of a family of highly conserved proteins within the Candidate Phyla Radiation. The function of CPR-C4 as a cysteine protease was predicted through remote structural similarity to the Homo sapiens vasohibins and subsequently confirmed experimentally with fluorescence-based activity assays. Furthermore, detailed structural and sequence alignment analysis enabled identification of a noncanonical cysteine-histidine-leucine(carbonyl) catalytic triad. The unexpected structural and functional similarities between CPR-C4 and the human vasohibins suggest an evolutionary relationship undetectable at the sequence level alone.

PubMed: 35405098
DOI: 10.1016/j.jbc.2022.101919

実験手法

X-RAY DIFFRACTION (2.248 Å)