6PBU

ClpP1 from Mycobacterium smegmatis

6PBU の概要

• エントリーDOI: 10.2210/pdb6pbu/pdb
• 分子名称: ATP-dependent Clp protease proteolytic subunit, MALONATE ION (3 entities in total)
• 機能のキーワード: protease, degradation, aaa+ unfoldase, hydrolase
• 由来する生物種: Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
• タンパク質・核酸の鎖数: 7
• 化学式量合計: 165212.42

構造登録者

Heras, B.,Nagpal, J.,Dougan, D.A. (登録日: 2019-06-14, 公開日: 2019-12-18, 最終更新日: 2023-10-11)

主引用文献

Nagpal, J.,Paxman, J.J.,Zammit, J.E.,Alhuwaider, A.,Truscott, K.N.,Heras, B.,Dougan, D.A.
Molecular and structural insights into an asymmetric proteolytic complex (ClpP1P2) from Mycobacterium smegmatis.
Sci Rep, 9:18019-18019, 2019

PubMed Abstract: The ClpP protease is found in all kingdoms of life, from bacteria to humans. In general, this protease forms a homo-oligomeric complex composed of 14 identical subunits, which associates with its cognate ATPase in a symmetrical manner. Here we show that, in contrast to this general architecture, the Clp protease from Mycobacterium smegmatis (Msm) forms an asymmetric hetero-oligomeric complex ClpP1P2, which only associates with its cognate ATPase through the ClpP2 ring. Our structural and functional characterisation of this complex demonstrates that asymmetric docking of the ATPase component is controlled by both the composition of the ClpP1 hydrophobic pocket (Hp) and the presence of a unique C-terminal extension in ClpP1 that guards this Hp. Our structural analysis of ClpP1 also revealed openings in the side-walls of the inactive tetradecamer, which may represent sites for product egress.

PubMed: 31792243
DOI: 10.1038/s41598-019-53736-8

実験手法

X-RAY DIFFRACTION (2 Å)