1MBU

Crystal Structure Analysis of ClpSN heterodimer

1MBU の概要

• エントリーDOI: 10.2210/pdb1mbu/pdb
• 関連するPDBエントリー: 1MBV 1MBX
• 分子名称: ATP-Dependent clp Protease ATP-Binding Subunit clp A, Protein yljA, BIS-(2-HYDROXYETHYL)AMINO-TRIS(HYDROXYMETHYL)METHANE YTTRIUM, ... (6 entities in total)
• 機能のキーワード: protein binding
• 由来する生物種: Escherichia coli; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 57919.90

構造登録者

Guo, F.,Esser, L.,Singh, S.K.,Maurizi, M.R.,Xia, D. (登録日: 2002-08-03, 公開日: 2002-12-11, 最終更新日: 2024-02-14)

主引用文献

Guo, F.,Esser, L.,Singh, S.K.,Maurizi, M.R.,Xia, D.
Crystal Structure of the Heterodimeric Complex of the Adaptor, ClpS, with the N-domain of the AAA+ Chaperone, ClpA
J.Biol.Chem., 277:46753-46762, 2002

PubMed Abstract: Substrate selectivity and proteolytic activity for the E. coli ATP-dependent protease, ClpAP, is modulated by an adaptor protein, ClpS. ClpS binds to ClpA, the regulatory component of the ClpAP complex. We report the crystal structure of ClpS in complex with the isolated N-terminal domain of ClpA in two different crystal forms at 2.3- and 3.3-A resolution. The ClpS structure forms an alpha/beta-sandwich and is topologically analogous to the C-terminal domain of the ribosomal protein L7/L12. ClpS contacts two surfaces on the N-terminal domain in both crystal forms; the more extensive interface was shown to be favored in solution by protease protection experiments. The N-terminal 20 residues of ClpS are not visible in the crystal structures; the removal of the first 17 residues produces ClpSDeltaN, which binds to the ClpA N-domain but no longer inhibits ClpA activity. A zinc binding site involving two His and one Glu residue was identified crystallographically in the N-terminal domain of ClpA. In a model of ClpS bound to hexameric ClpA, ClpS is oriented with its N terminus directed toward the distal surface of ClpA, suggesting that the N-terminal region of ClpS may affect productive substrate interactions at the apical surface or substrate entry into the ClpA translocation channel.

PubMed: 12235156
DOI: 10.1074/jbc.M208104200

実験手法

X-RAY DIFFRACTION (2.3 Å)