5i5l

The 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

spinqualitylabelsall models 5i5l, resolution 2.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5i5l is a 1 chain structure with sequence from Agrobacterium fabrum str. C58. This structure supersedes the now removed PDB entry 4wkk. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.7Å Ligands: BLA, CA, GOL, TAM Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q7CY45_AGRFC Publication Abstract from PubMed 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 Pr and Pfr states. These changes include secondary structure rearrangements in the so-called tongue of the PHY domain and structural rearrangements within the long alpha-helix that connects the GAF and the PHY domains. We present the crystal structures of the PCM of Agp1 at 2.70 A resolution and of a surface-engineered mutant of this PCM at 1.85 A 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 alpha-helix and the tongue, indicating pronounced structural flexibility which 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 Pro461 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. The Crystal Structures of the N-Terminal Photosensory Core Module of Agrobacterium Phytochrome Agp1 as Parallel and Anti-Parallel Dimers.,Nagano S, Scheerer P, Zubow K, Michael N, Inomata K, Lamparter T, Krauss N J Biol Chem. 2016 Jul 26. pii: jbc.M116.739136. PMID:27466363 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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