5HSQ

The surface engineered photosensory module (PAS-GAF-PHY) of the bacterial phytochrome Agp1 (AtBphP1) in the Pr form, chromophore modelled with an endocyclic double bond in pyrrole ring A.

5HSQ の概要

• エントリーDOI: 10.2210/pdb5hsq/pdb
• 分子名称: Bacteriophytochrome protein, BILIVERDINE IX ALPHA, CALCIUM ION, ... (6 entities in total)
• 機能のキーワード: surface mutations, bilin chromophore, photoisomerization, signaling protein
• 由来する生物種: Agrobacterium fabrum
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 55520.85

構造登録者

Nagano, S.,Scheerer, P.,Zubow, K.,Lamparter, T.,Krauss, N. (登録日: 2016-01-26, 公開日: 2016-08-03, 最終更新日: 2024-11-20)

主引用文献

Nagano, S.,Scheerer, P.,Zubow, K.,Michael, N.,Inomata, K.,Lamparter, T.,Krau, N.
The Crystal Structures of the N-terminal Photosensory Core Module of Agrobacterium Phytochrome Agp1 as Parallel and Anti-parallel Dimers.
J.Biol.Chem., 291:20674-20691, 2016

PubMed Abstract: Agp1 is a canonical biliverdin-binding bacteriophytochrome from the soil bacterium Agrobacterium fabrum that acts as a light-regulated histidine kinase. Crystal structures of the photosensory core modules (PCMs) of homologous phytochromes have provided a consistent picture of the structural changes that these proteins undergo during photoconversion between the parent red light-absorbing state (Pr) and the far-red light-absorbing state (Pfr). These changes include secondary structure rearrangements in the so-called tongue of the phytochrome-specific (PHY) domain and structural rearrangements within the long α-helix that connects the cGMP-specific phosphodiesterase, adenylyl cyclase, and FhlA (GAF) and the PHY domains. We present the crystal structures of the PCM of Agp1 at 2.70 Å resolution and of a surface-engineered mutant of this PCM at 1.85 Å resolution in the dark-adapted Pr states. Whereas in the mutant structure the dimer subunits are in anti-parallel orientation, the wild-type structure contains parallel subunits. The relative orientations between the PAS-GAF bidomain and the PHY domain are different in the two structures, due to movement involving two hinge regions in the GAF-PHY connecting α-helix and the tongue, indicating pronounced structural flexibility that may give rise to a dynamic Pr state. The resolution of the mutant structure enabled us to detect a sterically strained conformation of the chromophore at ring A that we attribute to the tight interaction with Pro-461 of the conserved PRXSF motif in the tongue. Based on this observation and on data from mutants where residues in the tongue region were replaced by alanine, we discuss the crucial roles of those residues in Pr-to-Pfr photoconversion.

PubMed: 27466363
DOI: 10.1074/jbc.M116.739136

実験手法

X-RAY DIFFRACTION (1.85 Å)