4QHJ

Crystal structure of Methanocaldococcus jannaschii selecase mutant I100F+H107F

4QHJ の概要

• エントリーDOI: 10.2210/pdb4qhj/pdb
• 関連するPDBエントリー: 4JIU 4JIX 4QHF 4QHG 4QHH 4QHI
• 分子名称: Uncharacterized protein MJ1213, ZINC ION, ACETATE ION, ... (5 entities in total)
• 機能のキーワード: minigluzincin, proteolytic enzyme, hydrolase
• 由来する生物種: Methanocaldococcus jannaschii
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 26811.31

構造登録者

Lopez-pelegrin, M.,Cerda-costa, N.,Cintas-pedrola, A.,Herranz-trillo, F.,Bernado, P.,Peinado, J.R.,Arolas, J.L.,Gomis-ruth, F.X. (登録日: 2014-05-28, 公開日: 2014-07-16, 最終更新日: 2024-04-03)

主引用文献

Lopez-Pelegrin, M.,Cerda-Costa, N.,Cintas-Pedrola, A.,Herranz-Trillo, F.,Bernado, P.,Peinado, J.R.,Arolas, J.L.,Gomis-Ruth, F.X.
Multiple stable conformations account for reversible concentration-dependent oligomerization and autoinhibition of a metamorphic metallopeptidase
Angew.Chem.Int.Ed.Engl., 53:10624-10630, 2014

PubMed Abstract: Molecular plasticity controls enzymatic activity: the native fold of a protein in a given environment is normally unique and at a global free-energy minimum. Some proteins, however, spontaneously undergo substantial fold switching to reversibly transit between defined conformers, the "metamorphic" proteins. Here, we present a minimal metamorphic, selective, and specific caseinolytic metallopeptidase, selecase, which reversibly transits between several different states of defined three-dimensional structure, which are associated with loss of enzymatic activity due to autoinhibition. The latter is triggered by sequestering the competent conformation in incompetent but structured dimers, tetramers, and octamers. This system, which is compatible with a discrete multifunnel energy landscape, affords a switch that provides a reversible mechanism of control of catalytic activity unique in nature.

PubMed: 25159620
DOI: 10.1002/anie.201405727

実験手法

X-RAY DIFFRACTION (1.75 Å)