Exploring Chromophore-Binding Pocket: High-Resolution Solid-State 1H–13C Interfacial Correlation NMR Spectra with Windowed PMLG Scheme

Song, Chen; Lang, Christina; Mailliet, Jo; Hughes, Jon; Gärtner, Wolfgang; Matysik, Jörg

doi:10.1007/s00723-011-0196-6

Cited by 6 publications

(7 citation statements)

References 55 publications

(75 reference statements)

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“…In conjunction with selective isotope labeling (i.e. chromophore labeled in total or at selected positions and of the protein at selected amino acid types) and irradiation techniques within the magnet, MAS NMR offers a particularly attractive route to study the photochemical machinery of photoreceptors down to the atomic level (46)(47)(48)(49)61,62).…”

Section: Mas Nmr Studies On Canonical Phytochromesmentioning

confidence: 99%

Solid‐State NMR Spectroscopy to Probe Photoactivation in Canonical Phytochromes

Song

Rohmer

Tiersch

et al. 2013

Photochem & Photobiology

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The photoreceptor phytochrome switches photochromically between two thermally stable states called Pr and Pfr. Here, we summarize recent solid-state magic-angle spinning (MAS) NMR work on this conversion process and interpret the functional mechanism in terms of a nano-machine. The process is initiated by a double-bond photoisomerization of the open-chain tetrapyrrole chromophore at the methine bridge connecting pyrrole rings C and D. The Pr-state chromophore and its surrounding pocket in canonical cyanobacterial and plant phytochromes has significantly less order, tends to form isoforms and is soft. Conversely, Pfr shows significantly harder chromophore-protein interactions, a well-defined protonic and charge distribution with a clear classical counterion for the positively charged tetrapyrrole system. The soft-tohard/disorder-to-order transition involves the chromophore and its protein surroundings within a sphere of at least 5.5 A. The relevance of this collective event for signaling is discussed. Measurement of the intermediates during the Pfr ? Pr back-reaction provides insight into the well-adjusted mechanics of a two-step transformation. As both Pr ? Pfr and Pfr ? Pr reaction pathways are different in ground and excited states, a photochemically controlled hyper-landscape is proposed allowing for ratchet-type reaction dynamics regulating signaling activity.

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Section: Mas Nmr Studies On Canonical Phytochromesmentioning

confidence: 99%

Solid‐State NMR Spectroscopy to Probe Photoactivation in Canonical Phytochromes

Song

Rohmer

Tiersch

et al. 2013

Photochem & Photobiology

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“…We present here the application of the solid-state MELODI-HETCOR technique (Song et al, 2011a(Song et al, , 2012 to the u-[ 13 C, 15 N]-PCB-As.phyA3(PAS-GAF-PHY) oat phytochrome A photosensor module in the Pr ground state. This method allows the labeled PCB carbons to probe the nearby amino acids located within a region of ;4.5 Å .…”

Section: Introductionmentioning

confidence: 99%

Solid-State NMR Spectroscopic Study of Chromophore–Protein Interactions in the Pr Ground State of Plant Phytochrome A

et al. 2012

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Despite extensive study, the molecular structure of the chromophore-binding pocket of phytochrome A (phyA), the principal photoreceptor controlling photomorphogenesis in plants, has not yet been successfully resolved. Here, we report a series of two-dimensional (2-D) magic-angle spinning solid-state NMR experiments on the recombinant N-terminal, 65-kDa PAS-GAF-PHY light-sensing module of phytochrome A3 from oat (Avena sativa), assembled with uniformly 13C- and 15N-labeled phycocyanobilin (u-[13C,15N]-PCB-As.phyA3). The Pr state of this protein was studied regarding the electronic structure of the chromophore and its interactions with the proximal amino acids. Using 2-D 13C-13C and 1H-15N experiments, a complete set of 13C and 15N assignments for the chromophore were obtained. Also, a large number of 1H-13C distance restraints between the chromophore and its binding pocket were revealed by interfacial heteronuclear correlation spectroscopy. 13C doublings of the chromophore A-ring region and the C-ring carboxylate moiety, together with the observation of two Pr isoforms, Pr-I and Pr-II, demonstrate the local mobility of the chromophore and the plasticity of its protein environment. It appears that the interactions and dynamics in the binding pocket of phyA in the Pr state are remarkably similar to those of cyanobacterial phytochrome (Cph1). The N-terminus of the region modeled (residues 56-66 of phyA) is highly mobile. Differences in the regulatory processes involved in plant and Cph1 phytochromes are discussed.

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“…There is a long list of crystal structures of bacterial phytochromes (see, for example, PDB entries 1ZTU, 2O9C, 2O9B, 3C2W, 3IBR, 3G6O, 3NHQ, 3S7P, 3S7O, 3S7N, 3S7Q, 3NOP, 3NOU, 3NOT, 4IJG, 4O0P, 4O01, 4CQH, 4GW9, 4E04, 4QOJ, 4QOI, 4QOH, 4O8G, 4Y5F, 4Y3I, 4XTQ, 4ZRR, 5Z1W, 5C5K, 5AJG, 5AKP, 4RQ9, 4RPW, 5HSQ, 5I5L, 5LBR, 5L8M, 5K5B, 5MBP, 5MBO), plant phytochrome (PDB entry 4OUR), or cyanobacterial phytochromes (PDB entries 2VEA, 3ZQ5, 3VV4, 4GLQ, 4BWI, 5DFY, 5DFX). These structural data are in some cases supported by electron microscopy , small angle X‐ray scattering (SAXS) and NMR measurements on the chromophore or on the entire protein (PDB entries 2K2N, 2KOI, 2KLI, 2LB9, 2LB5, 2M7U and 2M7V). Almost all crystal structures are from protein fragments and not from full‐length proteins.…”

Section: Crystal Structurementioning

confidence: 76%

“…The cyanobacterial phytochromes became the second “Standbein” of Wolfgang's phytochrome research . As a chemist, Wolfgang contributed by synthesis of artificial chromophores for the sake of labeling wherever it was necessary . Another major contribution was the establishment of recombinant expression of proteins .…”

Section: Introductionmentioning

confidence: 99%

Phytochromes from Agrobacterium fabrum

Lamparter

Krauß

Scheerer

2017

Photochem & Photobiology

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Agrobacterium fabrum is a widely used model bacterium for gene transfer from pro-to eukaryote, for genetics and metabolism. The phytochrome system of Agrobacterium, encompassing the two phytochromes Agp1 and Agp2, has provided deep insight into phytochrome action in a bacterial organism. This review summarizes recent results on phytochrome evolution, phytochrome regulation of conjugation and plant infection and biochemical studies including the crystal structure of Agp1-PCM, the photosensory core module of Agp1.

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Exploring Chromophore-Binding Pocket: High-Resolution Solid-State 1H–13C Interfacial Correlation NMR Spectra with Windowed PMLG Scheme

Cited by 6 publications

References 55 publications

Solid‐State NMR Spectroscopy to Probe Photoactivation in Canonical Phytochromes

Solid‐State NMR Spectroscopy to Probe Photoactivation in Canonical Phytochromes

Solid-State NMR Spectroscopic Study of Chromophore–Protein Interactions in the Pr Ground State of Plant Phytochrome A

Phytochromes from Agrobacterium fabrum

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