2WA9

Structural basis of N-end rule substrate recognition in Escherichia coli by the ClpAP adaptor protein ClpS - Trp peptide structure

2WA9 の概要

• エントリーDOI: 10.2210/pdb2wa9/pdb
• 関連するPDBエントリー: 1LZW 1MBU 1MBV 1MBX 1MG9 1R6O 1R6Q 2W9R 2WA8
• 分子名称: ATP-DEPENDENT CLP PROTEASE ADAPTER PROTEIN CLPS, TRP PEPTIDE (2 entities in total)
• 機能のキーワード: clps, clpa, clpp, n-end rule recognition, peptide-binding protein, peptide binding protein
• 由来する生物種: ESCHERICHIA COLI; 詳細
• タンパク質・核酸の鎖数: 14
• 化学式量合計: 88666.22

構造登録者

Schuenemann, V.J.,Kralik, S.M.,Albrecht, R.,Spall, S.K.,Truscott, K.N.,Dougan, D.A.,Zeth, K. (登録日: 2009-02-03, 公開日: 2009-04-28, 最終更新日: 2024-05-08)

主引用文献

Schuenemann, V.J.,Kralik, S.M.,Albrecht, R.,Spall, S.K.,Truscott, K.N.,Dougan, D.A.,Zeth, K.
Structural Basis of N-End Rule Substrate Recognition in Escherichia Coli by the Clpap Adaptor Protein Clps.
Embo Rep., 10:508-, 2009

PubMed Abstract: In Escherichia coli, the ClpAP protease, together with the adaptor protein ClpS, is responsible for the degradation of proteins bearing an amino-terminal destabilizing amino acid (N-degron). Here, we determined the three-dimensional structures of ClpS in complex with three peptides, each having a different destabilizing residue--Leu, Phe or Trp--at its N terminus. All peptides, regardless of the identity of their N-terminal residue, are bound in a surface pocket on ClpS in a stereo-specific manner. Several highly conserved residues in this binding pocket interact directly with the backbone of the N-degron peptide and hence are crucial for the binding of all N-degrons. By contrast, two hydrophobic residues define the volume of the binding pocket and influence the specificity of ClpS. Taken together, our data suggest that ClpS has been optimized for the binding and delivery of N-degrons containing an N-terminal Phe or Leu.

PubMed: 19373253
DOI: 10.1038/EMBOR.2009.62

実験手法

X-RAY DIFFRACTION (2.9 Å)