4WHE

Crystal structure of E. coli phage shock protein A (PspA 1-144)

4WHE の概要

• エントリーDOI: 10.2210/pdb4whe/pdb
• 分子名称: Phage shock protein A, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL (3 entities in total)
• 機能のキーワード: pspa/im30 family, aaa+ protein regulation, transcriptional regulation, stress inducible psp system, phage shock response, coiled-coil, sigma 54 promoter, transcription initiation, signaling protein
• 由来する生物種: Escherichia coli K-12
• 細胞内の位置: Cytoplasm : P0AFM7
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 17598.24

構造登録者

Parthier, C.,Schoepfel, M.,Stubbs, M.T.,Osadnik, H.,Brueser, T. (登録日: 2014-09-22, 公開日: 2015-09-02, 最終更新日: 2024-05-08)

主引用文献

Osadnik, H.,Schopfel, M.,Heidrich, E.,Mehner, D.,Lilie, H.,Parthier, C.,Risselada, H.J.,Grubmuller, H.,Stubbs, M.T.,Bruser, T.
PspF-binding domain PspA1-144 and the PspAF complex: New insights into the coiled-coil-dependent regulation of AAA+ proteins.
Mol.Microbiol., 98:743-759, 2015

PubMed Abstract: Phage shock protein A (PspA) belongs to the highy conserved PspA/IM30 family and is a key component of the stress inducible Psp system in Escherichia coli. One of its central roles is the regulatory interaction with the transcriptional activator of this system, the σ(54) enhancer-binding protein PspF, a member of the AAA+ protein family. The PspA/F regulatory system has been intensively studied and serves as a paradigm for AAA+ enzyme regulation by trans-acting factors. However, the molecular mechanism of how exactly PspA controls the activity of PspF and hence σ(54) -dependent expression of the psp genes is still unclear. To approach this question, we identified the minimal PspF-interacting domain of PspA, solved its structure, determined its affinity to PspF and the dissociation kinetics, identified residues that are potentially important for PspF regulation and analyzed effects of their mutation on PspF in vivo and in vitro. Our data indicate that several characteristics of AAA+ regulation in the PspA·F complex resemble those of the AAA+ unfoldase ClpB, with both proteins being regulated by a structurally highly conserved coiled-coil domain. The convergent evolution of both regulatory domains points to a general mechanism to control AAA+ activity for divergent physiologic tasks via coiled-coil domains.

PubMed: 26235546
DOI: 10.1111/mmi.13154

実験手法

X-RAY DIFFRACTION (1.8 Å)