1R6C

High resolution structure of ClpN

1R6C の概要

• エントリーDOI: 10.2210/pdb1r6c/pdb
• 関連するPDBエントリー: 1R6B 1R6O 1R6Q
• 分子名称: ATP-dependent Clp protease ATP-binding subunit clpA (2 entities in total)
• 機能のキーワード: clpa, aaa+, n-terminal domain, clps, crystal, binding mechanism, hydrolase
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 16200.27

構造登録者

Xia, D.,Maurizi, M.R.,Guo, F.,Singh, S.K.,Esser, L. (登録日: 2003-10-15, 公開日: 2005-02-15, 最終更新日: 2024-02-14)

主引用文献

Xia, D.,Esser, L.,Singh, S.K.,Guo, F.,Maurizi, M.R.
Crystallographic investigation of peptide binding sites in the N-domain of the ClpA chaperone
J.Struct.Biol., 146:166-179, 2004

PubMed Abstract: Escherichia coli ClpA, an Hsp100/Clp chaperone and an integral component of the ATP-dependent ClpAP protease, participates in the dissolution and degradation of regulatory proteins and protein aggregates. ClpA consists of three functional domains: an N-terminal domain and two ATPase domains, D1 and D2. The N-domain is attached to D1 by a mobile linker and is made up of two tightly bound, identically folded alpha-helical bundles related by a pseudo 2-fold symmetry. Between the halves of the pseudo-dimer is a large flexible acidic loop that becomes better ordered upon binding of the small adaptor protein, ClpS. We have identified a number of structural features in the N-domain, including a Zn(++) binding motif, several interfaces for binding to ClpS, and a prominent hydrophobic surface area that binds peptides in different configurations. These structural motifs may contribute to binding of protein or peptide substrates with weak affinity and broad specificity. Kinetic studies comparing wild-type ClpA to a mutant ClpA with its N-domain deleted show that the N-domains contribute to the binding of a non-specific protein substrate but not of a folded substrate with the specific SsrA recognition tag. A functional model is proposed in which the N-domains in ClpA function as tentacles to weakly hold on to proteins thereby enhancing local substrate concentration.

PubMed: 15037248
DOI: 10.1016/j.jsb.2003.11.025

実験手法

X-RAY DIFFRACTION (2.15 Å)