5BRJ

Structure of the bacteriophytochrome response regulator AtBRR

5BRJ の概要

• エントリーDOI: 10.2210/pdb5brj/pdb
• 分子名称: Two component response regulator, MAGNESIUM ION (3 entities in total)
• 機能のキーワード: bacteriophytochrome, response regulator, stable dimer, two component system, signaling protein
• 由来する生物種: Agrobacterium tumefaciens CCNWGS0286
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 15819.37

構造登録者

Baker, A.W.,Satyshur, K.A.,Forest, K.T. (登録日: 2015-05-31, 公開日: 2016-02-24, 最終更新日: 2024-03-06)

主引用文献

Baker, A.W.,Satyshur, K.A.,Moreno Morales, N.,Forest, K.T.
Arm-in-Arm Response Regulator Dimers Promote Intermolecular Signal Transduction.
J.Bacteriol., 198:1218-1229, 2016

PubMed Abstract: Bacteriophytochrome photoreceptors (BphPs) and their cognate response regulators make up two-component signal transduction systems which direct bacteria to mount phenotypic responses to changes in environmental light quality. Most of these systems utilize single-domain response regulators to transduce signals through unknown pathways and mechanisms. Here we describe the photocycle and autophosphorylation kinetics of RtBphP1, a red light-regulated histidine kinase from the desert bacterium Ramlibacter tataouinensis RtBphP1 undergoes red to far-red photoconversion with rapid thermal reversion to the dark state. RtBphP1 is autophosphorylated in the dark; this activity is inhibited under red light. The RtBphP1 cognate response regulator, the R. tataouinensis bacteriophytochrome response regulator (RtBRR), and a homolog, AtBRR from Agrobacterium tumefaciens, crystallize unexpectedly as arm-in-arm dimers, reliant on a conserved hydrophobic motif, hFWAhL (where h is a hydrophobic M, V, L, or I residue). RtBRR and AtBRR dimerize distinctly from four structurally characterized phytochrome response regulators found in photosynthetic organisms and from all other receiver domain homodimers in the Protein Data Bank. A unique cacodylate-zinc-histidine tag metal organic framework yielded single-wavelength anomalous diffraction phases and may be of general interest. Examination of the effect of the BRR stoichiometry on signal transduction showed that phosphorylated RtBRR is accumulated more efficiently than the engineered monomeric RtBRR (RtBRRmon) in phosphotransfer reactions. Thus, we conclude that arm-in-arm dimers are a relevant signaling intermediate in this class of two-component regulatory systems.

PubMed: 26833410
DOI: 10.1128/JB.00872-15

実験手法

X-RAY DIFFRACTION (1.922 Å)