5E7S

Hexameric structure of a LonA protease domain in active state

5E7S の概要

• エントリーDOI: 10.2210/pdb5e7s/pdb
• 分子名称: Lon protease (1 entity in total)
• 機能のキーワード: aaa+ domain, lon protease, protease domain, hydrolase
• 由来する生物種: Meiothermus taiwanensis
• 細胞内の位置: Cytoplasm : A0A059VAZ3
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 391252.15

構造登録者

Lin, C.-C.,Su, S.-C.,Chang, C.-I. (登録日: 2015-10-13, 公開日: 2016-03-16, 最終更新日: 2023-11-08)

主引用文献

Su, S.-C.,Lin, C.-C.,Tai, H.-C.,Chang, M.-Y.,Ho, M.-R.,Babu, C.S.,Liao, J.-H.,Wu, S.-H.,Chang, Y.-C.,Lim, C.,Chang, C.-I.
Structural Basis for the Magnesium-Dependent Activation and Hexamerization of the Lon AAA+ Protease
Structure, 24:676-686, 2016

PubMed Abstract: The Lon AAA+ protease (LonA) plays important roles in protein homeostasis and regulation of diverse biological processes. LonA behaves as a homomeric hexamer in the presence of magnesium (Mg(2+)) and performs ATP-dependent proteolysis. However, it is also found that LonA can carry out Mg(2+)-dependent degradation of unfolded protein substrate in an ATP-independent manner. Here we show that in the presence of Mg(2+) LonA forms a non-secluded hexameric barrel with prominent openings, which explains why Mg(2+)-activated LonA can operate as a diffusion-based chambered protease to degrade unstructured protein and peptide substrates efficiently in the absence of ATP. A 1.85 Å crystal structure of Mg(2+)-activated protease domain reveals Mg(2+)-dependent remodeling of a substrate-binding loop and a potential metal-binding site near the Ser-Lys catalytic dyad, supported by biophysical binding assays and molecular dynamics simulations. Together, these findings reveal the specific roles of Mg(2+) in the molecular assembly and activation of LonA.

PubMed: 27041593
DOI: 10.1016/j.str.2016.03.003

実験手法

X-RAY DIFFRACTION (3.03 Å)