2CE3

CRYSTAL STRUCTURE OF THE ATP-DEPENDENT CLP PROTEASE PROTEOLYTIC SUBUNIT 1 (CLPP1) FROM MYCOBACTERIUM TUBERCULOSIS

2CE3 の概要

• エントリーDOI: 10.2210/pdb2ce3/pdb
• 関連するPDBエントリー: 2C8T 2CBY
• 分子名称: ATP-DEPENDENT CLP PROTEASE PROTEOLYTIC SUBUNIT 1 (2 entities in total)
• 機能のキーワード: serine protease, clp protease, proteolytic subunit, endopeptidase, mycobacterium tuberculosis, atp-dependent protease, hydrolase
• 由来する生物種: MYCOBACTERIUM TUBERCULOSIS (KOCH'S BACILLUS)
• タンパク質・核酸の鎖数: 14
• 化学式量合計: 304187.30

構造登録者

Segelke, B.,Kim, C.Y.,Ortiz-Lombardia, M.,Alzari, P.M.,Lekin, T. (登録日: 2006-02-03, 公開日: 2006-02-09, 最終更新日: 2023-12-13)

主引用文献

Ingvarsson, H.,Mate, M.J.,Hogbom, M.,Portnoi, D.,Benaroudj, N.,Alzari, P.M.,Ortiz-Lombardia, M.,Unge, T.
Insights Into the Inter-Ring Plasticity of Caseinolytic Proteases from the X-Ray Structure of Mycobacterium Tuberculosis Clpp1.
Acta Crystallogr.,Sect.D, 63:249-, 2007

PubMed Abstract: Mycobacterium tuberculosis caseinolytic protease ClpP1 (Mt ClpP1) is a self-compartmentalized protease consisting of two heptameric rings stacked on top of each other, thus enclosing a catalytic chamber. Within the chamber, which can be reached through two axial pores, each of the 14 identical monomers possesses a serine protease active site. The unfolding and translocation of substrates into the chamber are mediated by associated hexameric ATPases covering the axial pores. Three crystal structures of Mt ClpP1, determined by molecular replacement, are presented in this study. Two of the models were refined to a resolution of 2.6 A and the third to 3.0 A. It was found that disorder in the handle domain affects the formation and configuration of the tetradecamer and results in condensed structures with larger equatorial pores when compared with ClpPs from other species. Additionally, this disorder accompanies conformational changes of the residues in the catalytic triad. The models also reveal structural differences within the N-terminal hairpin-loop domain, which possibly reflect the significant differences in amino-acid sequence between Mt ClpP1 and other ClpP homologues in this region.

PubMed: 17242518
DOI: 10.1107/S0907444906050530

実験手法

X-RAY DIFFRACTION (2.6 Å)