4L9E

Structure of PpsR Q-PAS1 from Rb. sphaeroides

4L9E の概要

• エントリーDOI: 10.2210/pdb4l9e/pdb
• 関連するPDBエントリー: 4HH0 4HH2 4HH3 4L9F 4L9G
• 分子名称: Transcriptional regulator, PpsR (2 entities in total)
• 機能のキーワード: pas domain, per-arnt-sim, oligomerization, transcription
• 由来する生物種: Rhodobacter sphaeroides
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 15319.64

構造登録者

Heintz, U.,Meinhart, A.,Schlichting, I.,Winkler, A. (登録日: 2013-06-18, 公開日: 2014-02-12, 最終更新日: 2023-09-20)

主引用文献

Heintz, U.,Meinhart, A.,Winkler, A.
Multi-PAS domain-mediated protein oligomerization of PpsR from Rhodobacter sphaeroides.
Acta Crystallogr.,Sect.D, 70:863-876, 2014

PubMed Abstract: Per-ARNT-Sim (PAS) domains are essential modules of many multi-domain signalling proteins that mediate protein interaction and/or sense environmental stimuli. Frequently, multiple PAS domains are present within single polypeptide chains, where their interplay is required for protein function. Although many isolated PAS domain structures have been reported over the last decades, only a few structures of multi-PAS proteins are known. Therefore, the molecular mechanism of multi-PAS domain-mediated protein oligomerization and function is poorly understood. The transcription factor PpsR from Rhodobacter sphaeroides is such a multi-PAS domain protein that, in addition to its three PAS domains, contains a glutamine-rich linker and a C-terminal helix-turn-helix DNA-binding motif. Here, crystal structures of two N-terminally and C-terminally truncated PpsR variants that comprise a single (PpsRQ-PAS1) and two (PpsRN-Q-PAS1) PAS domains, respectively, are presented and the multi-step strategy required for the phasing of a triple PAS domain construct (PpsRΔHTH) is illustrated. While parts of the biologically relevant dimerization interface can already be observed in the two shorter constructs, the PpsRΔHTH structure reveals how three PAS domains enable the formation of multiple oligomeric states (dimer, tetramer and octamer), highlighting that not only the PAS cores but also their α-helical extensions are essential for protein oligomerization. The results demonstrate that the long helical glutamine-rich linker of PpsR results from a direct fusion of the N-cap of the PAS1 domain with the C-terminal extension of the N-domain that plays an important role in signal transduction.

PubMed: 24598755
DOI: 10.1107/S1399004713033634

実験手法

X-RAY DIFFRACTION (1.65 Å)