3HLN

Crystal structure of ClpP A153C mutant with inter-heptamer disulfide bonds

3HLN の概要

• エントリーDOI: 10.2210/pdb3hln/pdb
• 分子名称: ATP-dependent Clp protease proteolytic subunit, CALCIUM ION (2 entities in total)
• 機能のキーワード: disulfide bond, disordered equatorial loops, atp-binding, hydrolase, nucleotide-binding, protease, serine protease, stress response, zymogen
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cytoplasm: P0A6G7
• タンパク質・核酸の鎖数: 28
• 化学式量合計: 605851.00

構造登録者

Kimber, M.S.,Yu, A.Y.H.,Borg, M.,Chan, H.S.,Houry, W.A. (登録日: 2009-05-27, 公開日: 2010-07-28, 最終更新日: 2024-11-06)

主引用文献

Kimber, M.S.,Yu, A.Y.,Borg, M.,Leung, E.,Chan, H.S.,Houry, W.A.
Structural and Theoretical Studies Indicate that the Cylindrical Protease ClpP Samples Extended and Compact Conformations.
Structure, 18:798-808, 2010

PubMed Abstract: The highly conserved ClpP protease consists of two heptameric rings that interact by the interdigitation of an alpha-helix beta strand handle domain motif to form a tetradecameric cylinder. We previously proposed that protease dynamics results in the temporary unstructuring of interacting pairs of handle domains, opening transient equatorial side pores that allow for peptide egress. Here, we report the structure of an Escherichia coli ClpP mutant in which each opposing pair of protomers is linked by a disulfide bond. This structure resembles the compact structures of Streptococcus pneumoniae, Mycobacterium tuberculosis, and Plasmodium falciparum ClpPs, rather than the active, extended structures that have previously been determined for E. coli ClpPs. The structural data, along with normal mode analysis, support a model whereby the ClpP cylinder switches dynamically between an active extended state required for substrate degradation and an inactive compact state allowing peptide product release.

PubMed: 20637416
DOI: 10.1016/j.str.2010.04.008

実験手法

X-RAY DIFFRACTION (3.2 Å)