4HH1

Dark-state structure of AppA wild-type without the Cys-rich region from Rb. sphaeroides

4HH1 の概要

• エントリーDOI: 10.2210/pdb4hh1/pdb
• 関連するPDBエントリー: 1YRX 2IYG 2IYI 4HH0 4HH2 4HH3
• 分子名称: AppA protein, FLAVIN MONONUCLEOTIDE (2 entities in total)
• 機能のキーワード: bluf domain, schic domain, photoreceptor, ppsr, flavoprotein, signaling protein
• 由来する生物種: Rhodobacter sphaeroides (Rhodopseudomonas sphaeroides)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 88662.73

構造登録者

Winkler, A.,Heintz, U.,Lindner, R.,Reinstein, J.,Shoeman, R.,Schlichting, I. (登録日: 2012-10-09, 公開日: 2013-06-05, 最終更新日: 2024-02-28)

主引用文献

Winkler, A.,Heintz, U.,Lindner, R.,Reinstein, J.,Shoeman, R.L.,Schlichting, I.
A ternary AppA-PpsR-DNA complex mediates light regulation of photosynthesis-related gene expression.
Nat.Struct.Mol.Biol., 20:859-867, 2013

PubMed Abstract: The anoxygenic phototrophic bacterium Rhodobacter sphaeroides uses different energy sources, depending on environmental conditions including aerobic respiration or, in the absence of oxygen, photosynthesis. Photosynthetic genes are repressed at high oxygen tension, but at intermediate levels their partial expression prepares the bacterium for using light energy. Illumination, however, enhances repression under semiaerobic conditions. Here, we describe molecular details of two proteins mediating oxygen and light control of photosynthesis-gene expression: the light-sensing antirepressor AppA and the transcriptional repressor PpsR. Our crystal structures of both proteins and their complex and hydrogen/deuterium-exchange data show that light activation of AppA-PpsR2 affects the PpsR effector region within the complex. DNA binding studies demonstrate the formation of a light-sensitive ternary AppA-PpsR-DNA complex. We discuss implications of these results for regulation by light and oxygen, highlighting new insights into blue light-mediated signal transduction.

PubMed: 23728293
DOI: 10.1038/nsmb.2597

実験手法

X-RAY DIFFRACTION (3.501 Å)