9RN8
Crystal structure of the photosensory core module (PCM) of a cyano-phenylalanine mutant oCNF205 of the bathy phytochrome Agp2 from Agrobacterium fabrum in the Pfr state.
Summary for 9RN8
| Entry DOI | 10.2210/pdb9rn8/pdb |
| Related | 6G1Y 6G1Z 6G20 8RFP 8RJM 8RJN 8RJO 8RJQ 8RJR 8RJS 8RJT 8RJU 9G8C 9G8D |
| Descriptor | histidine kinase, 3-[(2Z)-2-({3-(2-carboxyethyl)-5-[(E)-(4-ethenyl-3-methyl-5-oxo-1,5-dihydro-2H-pyrrol-2-ylidene)methyl]-4-methyl-1H-pyrrol-2-yl}methylidene)-5-{(Z)-[(3E,4S)-3-ethylidene-4-methyl-5-oxopyrrolidin-2-ylidene]methyl}-4-methyl-2H-pyrrol-3-yl]propanoic acid, (4S)-2-METHYL-2,4-PENTANEDIOL, ... (8 entities in total) |
| Functional Keywords | fluorescent protein, phytochrome, bacteriophytochrome, pfr-state, ortho-cyano-phenylalanine, stark labels, signaling protein |
| Biological source | Agrobacterium fabrum str. C58 More |
| Total number of polymer chains | 2 |
| Total formula weight | 115301.11 |
| Authors | |
| Primary citation | La Greca, M.,Nguyen, A.D.,Kraskov, A.,Michael, N.,Sauthof, L.,Ebrahim, M.,Katz, S.,von Sass, J.,Hoang, O.T.,Budisa, N.,Scheerer, P.,Schlesinger, R.,Mroginski, M.A.,Hildebrandt, P. Propagation of Photoinduced Electric Field Changes Through Phytochrome and their Impact on Conformational Transitions. Chemphyschem, :e202500595-e202500595, 2025 Cited by PubMed Abstract: In phytochromes, photoisomerization of the chromophore and subsequent structural relaxations lead to the functionally essential secondary structure transition of the tongue, a phytochrome-specific protein segment. The coupling mechanism between chromophore and protein structural changes is yet not understood, but electric field changes are discussed to play an important role. In this work, electric field changes in the chromophore binding pocket (CBP) are confirmed to propagate over long distances through the protein and alter the electric field in the tongue region. An experimental-theoretical approach to analyze local electric fields using Stark reporters has been further developed. These are nitrile groups introduced site-specifically into the protein via noncanonical amino acids. The functional integrity of the variants is checked by crystallography and various spectroscopies. For the first time, functionally intact variants with substitutions in the tongue are generated. Based on frequency shifts and relative intensities of the nitrile stretching modes, hydrogen-bonding and noncovalent electric field contributions are separated. The field changes originating in the CBP are transduced to the tongue along a pathway via Phe192. Given a proper direction of the net electric field vector in the tongue region, the magnitude of the field may be sufficient to destabilize the tongue structure. PubMed: 40976591DOI: 10.1002/cphc.202500595 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.79 Å) |
Structure validation
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