1UM8

Crystal structure of helicobacter pylori ClpX

1UM8 の概要

• エントリーDOI: 10.2210/pdb1um8/pdb
• 分子名称: ATP-dependent Clp protease ATP-binding subunit clpX, ADENOSINE-5'-DIPHOSPHATE (3 entities in total)
• 機能のキーワード: clpp binding loop, chaperone
• 由来する生物種: Helicobacter pylori
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 42518.76

構造登録者

Kim, D.Y.,Kim, K.K. (登録日: 2003-09-25, 公開日: 2003-12-23, 最終更新日: 2023-12-27)

主引用文献

Kim, D.Y.,Kim, K.K.
Crystal Structure of ClpX Molecular Chaperone from Helicobacter pylori
J.Biol.Chem., 278:50664-50670, 2003

PubMed Abstract: ClpX, a heat shock protein 100 chaperone, which acts as the regulatory subunit of the ATP-dependent ClpXP protease, is responsible for intracellular protein remodeling and degradation. To provide a structural basis for a better understanding of the function of the Clp ATPase family, the crystal structures of Helicobacter pylori ClpX, lacking an N-terminal Cys cluster region complexed with ADP, was determined. The overall structure of ClpX is similar to that of heat shock locus U (HslU), consisting of two subdomains, with ADP bound at the subdomain interface. The crystal structure of ClpX reveals that a conserved tripeptide (LGF) is located on the tip of ClpP binding loop extending from the N-terminal subdomain. A hexameric model of ClpX suggests that six tripeptides make hydrophobic contacts with the hydrophobic clefts of the ClpP heptmer asymmetrically. In addition, the nucleotide binding environment provides the structural explanation for the hexameric assembly and the modulation of ATPase activity.

PubMed: 14514695
DOI: 10.1074/jbc.M305882200

実験手法

X-RAY DIFFRACTION (2.6 Å)