Spectroscopy and a High-Resolution Crystal Structure of Tyr263 Mutants of Cyanobacterial Phytochrome Cph1

Mailliet, Jo; Psakis, Georgios; Feilke, Kathleen; Sineshchekov, V.A.; Essen, Lars‐Oliver; Hughes, Jon

doi:10.1016/j.jmb.2011.08.023

Cited by 71 publications

(141 citation statements)

References 69 publications

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“…site like Tyr 133 are functionally similar to their structural counterparts in SynCph1 (Tyr 263 ) as indicated by the similar photochemistry of their mutants, for example, Y133F or H160A (supplemental Fig. S1 and Table S2) (37).…”

Section: Resultsmentioning

confidence: 74%

“…First, the new chiral center at C3 1 , as formed by covalent attachment to Cys 129 , has an R configuration. This may not be a general feature for bilin chromophores covalently tethered to GAF domains; for example, in the structure of the Y263F mutant of SynCph1 both stereochemical configurations have been found for the C3 1 -Cys thioether linkage (37). Second, and as expected, for the SynCph2(1-2) P r state, the chromophore adopts the ZZZssa conformation (Fig.…”

Section: Resultsmentioning

confidence: 79%

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Structure of the Cyanobacterial Phytochrome 2 Photosensor Implies a Tryptophan Switch for Phytochrome Signaling

Anders

Daminelli-Widany

Mroginski

et al. 2013

Journal of Biological Chemistry

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168

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Background: Phytochromes are red/far-red photoreceptors using a bilin chromophore. Results: Compared with Cph1, the Cph2 bilin-binding site differs around the propionates, but utilizes an otherwise conserved tongue for sealing the chromophore from solvent. Conclusion:The tongue signals via a tryptophan switch within the tongue-GAF domain interface. Significance: The first structure of a Cph2-type phytochrome indicates a common mechanism for photoswitching in all canonical phytochromes.

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Section: Resultsmentioning

confidence: 74%

Section: Resultsmentioning

confidence: 79%

Structure of the Cyanobacterial Phytochrome 2 Photosensor Implies a Tryptophan Switch for Phytochrome Signaling

Anders

Daminelli-Widany

Mroginski

et al. 2013

Journal of Biological Chemistry

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168

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“…However, PCB in ApcEΔ is exceptional in having, instead, the ZZZssa geometry (Figs. 3 and 4) that is characteristic for the photoactive bilin chromophores of the sensory photoreceptors, phytochromes, and cyanobacteriochromes (14)(15)(16)(17). The unusual ZZZssa geometry of PCB is stabilized in ApcEΔ by the pivotal carboxyl group of Asp161: the pyrrolic nitrogens of rings A, B, and C are in H-bonding positions [NH-O = 2.7 (ring A), NH-O = 2.9 (ring B), and NH-O = 2.8 Å (ring C)] (Fig.…”

Section: Resultsmentioning

confidence: 99%

“…4 and Table S2). There are only few examples of phytochromes or cyanobacteriochromes containing PCB (14)(15)(16)(17), but the trend is pronounced. Extrapolating from these values, the absorption maxima of the chromophores in chains A (Φ tot = 22°) and B (Φ tot = 35°) are both expected at ∼660 nm, despite their moderate deviation from coplanarity [definition of coplanarity (Φ tot ) is provided in legend of Fig.…”

Section: Resultsmentioning

confidence: 99%

“…These shifts and their intense fluorescence are brought about by noncovalent interactions with the apoproteins (13). The malleability of this flexible open-chain tetrapyrrole chromophore by the apoprotein is also further emphasized by its presence in sensory photoreceptors (phytochromes and cyanobacteriochromes), which serve as photoswitches (14)(15)(16)(17). Here, PCB shows only low fluorescence.…”

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The terminal phycobilisome emitter, L _CM : A light-harvesting pigment with a phytochrome chromophore

Tang

Ding

Höppner

et al. 2015

Proc. Natl. Acad. Sci. U.S.A.

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Photosynthesis relies on energy transfer from light-harvesting complexes to reaction centers. Phycobilisomes, the light-harvesting antennas in cyanobacteria and red algae, attach to the membrane via the multidomain core-membrane linker, L CM . The chromophore domain of L CM forms a bottleneck for funneling the harvested energy either productively to reaction centers or, in case of light overload, to quenchers like orange carotenoid protein (OCP) that prevent photodamage. The crystal structure of the solubly modified chromophore domain from Nostoc sp. PCC7120 was resolved at 2.2 Å. Although its protein fold is similar to the protein folds of phycobiliproteins, the phycocyanobilin (PCB) chromophore adopts ZZZssa geometry, which is unknown among phycobiliproteins but characteristic for sensory photoreceptors (phytochromes and cyanobacteriochromes). However, chromophore photoisomerization is inhibited in L CM by tight packing. The ZZZssa geometry of the chromophore and π-π stacking with a neighboring Trp account for the functionally relevant extreme spectral red shift of L CM . Exciton coupling is excluded by the large distance between two PCBs in a homodimer and by preservation of the spectral features in monomers. The structure also indicates a distinct flexibility that could be involved in quenching. The conclusions from the crystal structure are supported by femtosecond transient absorption spectra in solution.cyanobacteria | phycobilisome | core-membrane linker | photosynthesis | crystal structure T he structural separation of light-harvesting and energy transduction processes allows photosynthetic organisms a flexible adaptation to the diverse light regimes present in terrestrial and aqueous habitats. In cyanobacteria and some phylogenetically related organisms that, together, provide a substantial proportion of global carbon fixation, light is harvested by hundreds of chromophores located in the peripheral antenna, namely, the phycobilisome (PBS). These excitations are then collected and transferred to the energy-transducing photosystems I (PSI) and PSII in the photosynthetic membrane via only two pigments, allophycocyanin B (AP-B) and the core-membrane linker (L CM ) (1-5). AP-B preferentially serves PSI (2); it is structurally similar to the bulk phycobiliproteins of the PBS (6). L CM (denoted as ApcE according to the gene by which it is encoded), preferentially serving PSII (5), is a more complex multidomain protein, with an N-terminal section that binds the phycocyanobilin (PCB) chromophore, and is homologous to phycobiliproteins but carries an additional loop that probably acts as a membrane anchor to PSII (4, 7-10). The Cterminal section consists of two to four repeats (depending on the PBS type) that are homologous to the N-terminal domain (Pfam PF00427) of structural PBS proteins, rod-linkers [Protein Data Bank (PDB) ID codes 3OSJ and 3OHW], and considered to organize the complex PBS core (9). They are probably also the loci for phosphorylation (11).Both AP-B and L CM contain the same PCB chromophores...

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Benchmarking of Cph1 Mutants and DrBphP for Light‐Responsive Phytochrome‐Based Hydrogels with Reversibly Adjustable Mechanical Properties

et al. 2022

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In the rapidly expanding field of molecular optogenetics, the performance of the engineered systems relies on the switching properties of the underlying genetically encoded photoreceptors. In this study, the bacterial phytochromes Cph1 and DrBphP are engineered, recombinantly produced in Escherichia coli, and characterized regarding their switching properties in order to synthesize biohybrid hydrogels with increased light‐responsive stiffness modulations. The R472A mutant of the cyanobacterial phytochrome 1 (Cph1) is identified to confer the phytochrome‐based hydrogels with an increased dynamic range for the storage modulus but a different light‐response for the loss modulus compared to the original Cph1‐based hydrogel. Stiffness measurements of human atrial fibroblasts grown on these hydrogels suggest that differences in the loss modulus at comparable changes in the storage modulus affect cell stiffness and thus underline the importance of matrix viscoelasticity on cellular mechanotransduction. The hydrogels presented here are of interest for analyzing how mammalian cells respond to dynamic viscoelastic cues. Moreover, the Cph1‐R472A mutant, as well as the benchmarking of the other phytochrome variants, are expected to foster the development and performance of future optogenetic systems.

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Spectroscopy and a High-Resolution Crystal Structure of Tyr263 Mutants of Cyanobacterial Phytochrome Cph1

Cited by 71 publications

References 69 publications

Structure of the Cyanobacterial Phytochrome 2 Photosensor Implies a Tryptophan Switch for Phytochrome Signaling

Structure of the Cyanobacterial Phytochrome 2 Photosensor Implies a Tryptophan Switch for Phytochrome Signaling

The terminal phycobilisome emitter, L _CM : A light-harvesting pigment with a phytochrome chromophore

Benchmarking of Cph1 Mutants and DrBphP for Light‐Responsive Phytochrome‐Based Hydrogels with Reversibly Adjustable Mechanical Properties

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Spectroscopy and a High-Resolution Crystal Structure of Tyr263 Mutants of Cyanobacterial Phytochrome Cph1

Cited by 71 publications

References 69 publications

Structure of the Cyanobacterial Phytochrome 2 Photosensor Implies a Tryptophan Switch for Phytochrome Signaling

Structure of the Cyanobacterial Phytochrome 2 Photosensor Implies a Tryptophan Switch for Phytochrome Signaling

The terminal phycobilisome emitter, L CM : A light-harvesting pigment with a phytochrome chromophore

Benchmarking of Cph1 Mutants and DrBphP for Light‐Responsive Phytochrome‐Based Hydrogels with Reversibly Adjustable Mechanical Properties

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The terminal phycobilisome emitter, L _CM : A light-harvesting pigment with a phytochrome chromophore