1YFN

Versatile modes of peptide recognition by the AAA+ adaptor protein SspB- the crystal structure of a SspB-RseA complex

1YFN の概要

• エントリーDOI: 10.2210/pdb1yfn/pdb
• 関連するPDBエントリー: 1OU8 1OU9 1OUL 1OX8 1OX9
• 分子名称: Stringent starvation protein B, Sigma-E factor negative regulatory protein (3 entities in total)
• 機能のキーワード: protein-peptide complex, sspb, rsea, protein binding
• 由来する生物種: Escherichia coli; 詳細
• 細胞内の位置: Cell membrane; Single-pass membrane protein (Potential): P38106
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 67564.98

構造登録者

Levchenko, I.,Grant, R.A.,Flynn, J.M.,Sauer, R.T.,Baker, T.A. (登録日: 2005-01-03, 公開日: 2005-05-17, 最終更新日: 2023-08-23)

主引用文献

Levchenko, I.,Grant, R.A.,Flynn, J.M.,Sauer, R.T.,Baker, T.A.
Versatile modes of peptide recognition by the AAA+ adaptor protein SspB
Nat.Struct.Mol.Biol., 12:520-525, 2005

PubMed Abstract: Energy-dependent proteases often rely on adaptor proteins to modulate substrate recognition. The SspB adaptor binds peptide sequences in the stress-response regulator RseA and in ssrA-tagged proteins and delivers these molecules to the AAA+ ClpXP protease for degradation. The structure of SspB bound to an ssrA peptide is known. Here, we report the crystal structure of a complex between SspB and its recognition peptide in RseA. Notably, the RseA sequence is positioned in the peptide-binding groove of SspB in a direction opposite to the ssrA peptide, the two peptides share only one common interaction with the adaptor, and the RseA interaction site is substantially larger than the overlapping ssrA site. This marked diversity in SspB recognition of different target proteins indicates that it is capable of highly flexible and dynamic substrate delivery.

PubMed: 15880122
DOI: 10.1038/nsmb934

実験手法

X-RAY DIFFRACTION (1.8 Å)