6bak

The structure of the Stigmatella aurantiaca phytochrome chromophore binding domain T289H mutant

spinqualitylabelsall models 6bak, resolution 1.92Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6bak is a 1 chain structure with sequence from Stigmatella aurantiaca DW4/3-1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.92Å Ligands: BLR Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q097N3_STIAD Publication Abstract from PubMed Phytochromes are red-light photoreceptors that were first characterized in plants, with homologs in photosynthetic and non-photosynthetic bacteria known as bacteriophytochromes (BphPs). Upon absorption of light, BphPs interconvert between two states denoted Pr and Pfr with distinct absorption spectra in the red and far-red. They have recently been engineered as enzymatic photoswitches for fluorescent-marker applications in non-invasive tissue imaging of mammals. This article presents cryo- and room-temperature crystal structures of the unusual phytochrome from the non-photosynthetic myxo-bacterium Stigmatella aurantiaca (SaBphP1) and reveals its role in the fruiting-body formation of this photomorphogenic bacterium. SaBphP1 lacks a conserved histidine (His) in the chromophore-binding domain that stabilizes the Pr state in the classical BphPs. Instead it contains a threonine (Thr), a feature that is restricted to several myxobacterial phytochromes and is not evolutionarily understood. SaBphP1 structures of the chromophore binding domain (CBD) and the complete photosensory core module (PCM) in wild-type and Thr-to-His mutant forms reveal details of the molecular mechanism of the Pr/Pfr transition associated with the physiological response of this myxobacterium to red light. Specifically, key structural differences in the CBD and PCM between the wild-type and the Thr-to-His mutant involve essential chromophore contacts with proximal amino acids, and point to how the photosignal is transduced through the rest of the protein, impacting the essential enzymatic activity in the photomorphogenic response of this myxobacterium. Structural basis for light control of cell development revealed by crystal structures of a myxobacterial phytochrome.,Woitowich NC, Halavaty AS, Waltz P, Kupitz C, Valera J, Tracy G, Gallagher KD, Claesson E, Nakane T, Pandey S, Nelson G, Tanaka R, Nango E, Mizohata E, Owada S, Tono K, Joti Y, Nugent AC, Patel H, Mapara A, Hopkins J, Duong P, Bizhga D, Kovaleva SE, St Peter R, Hernandez CN, Ozarowski WB, Roy-Chowdhuri S, Yang JH, Edlund P, Takala H, Ihalainen J, Brayshaw J, Norwood T, Poudyal I, Fromme P, Spence JCH, Moffat K, Westenhoff S, Schmidt M, Stojkovic EA IUCrJ. 2018 Aug 29;5(Pt 5):619-634. doi: 10.1107/S2052252518010631. eCollection, 2018 Sep 1. PMID:30224965 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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