1Y7O

The structure of Streptococcus pneumoniae A153P ClpP

1Y7O の概要

• エントリーDOI: 10.2210/pdb1y7o/pdb
• 分子名称: ATP-dependent Clp protease proteolytic subunit, CALCIUM ION (3 entities in total)
• 機能のキーワード: protease, hydrolase
• 由来する生物種: Streptococcus pneumoniae
• タンパク質・核酸の鎖数: 7
• 化学式量合計: 170284.73

構造登録者

Kimber, M.S.,Gribun, A.,Ching, R.,Sprangers, R.,Fiebig, K.M.,Houry, W.A. (登録日: 2004-12-09, 公開日: 2005-02-08, 最終更新日: 2024-11-13)

主引用文献

Gribun, A.,Kimber, M.S.,Ching, R.,Sprangers, R.,Fiebig, K.M.,Houry, W.A.
The ClpP double ring tetradecameric protease exhibits plastic ring-ring interactions, and the N termini of its subunits form flexible loops that are essential for ClpXP and ClpAP complex formation.
J.Biol.Chem., 280:16185-16196, 2005

PubMed Abstract: ClpP is a conserved serine-protease with two heptameric rings that enclose a large chamber containing the protease active sites. Each ClpP subunit can be divided into a handle region, which mediates ring-ring interactions, and a head domain. ClpP associates with the hexameric ATPases ClpX and ClpA, which can unfold and translocate substrate proteins through the ClpP axial pores into the protease lumen for degradation. We have determined the x-ray structure of Streptococcus pneumoniae ClpP(A153P) at 2.5 A resolution. The structure revealed two novel features of ClpP which are essential for ClpXP and ClpAP functional activities. First, the Ala --> Pro mutation disrupts the handle region, resulting in an altered ring-ring dimerization interface, which, in conjunction with biochemical data, demonstrates the unusual plasticity of this region. Second, the structure shows the existence of a flexible N-terminal loop in each ClpP subunit. The loops line the axial pores in the ClpP tetradecamer and then protrude from the protease apical surface. The sequence of the N-terminal loop is highly conserved in ClpP across all kingdoms of life. These loops are essential determinants for complex formation between ClpP and ClpX/ClpA. Mutation of several amino acid residues in this loop or the truncation of the loop impairs ClpXP and ClpAP complex formation and prevents the coupling between ClpX/ClpA and ClpP activities.

PubMed: 15701650
DOI: 10.1074/jbc.M414124200

実験手法

X-RAY DIFFRACTION (2.51 Å)