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5J4E

Crystal structures reveal signaling states of a short blue light photoreceptor protein PpSB1-LOV (Photoexcited state)

Summary for 5J4E
Entry DOI10.2210/pdb5j4e/pdb
DescriptorSensory box protein, FLAVIN MONONUCLEOTIDE (2 entities in total)
Functional Keywordssignaling protein, lov domain
Biological sourcePseudomonas putida
Total number of polymer chains4
Total formula weight76296.70
Authors
Granzin, J.,Batra-Safferling, R. (deposition date: 2016-04-01, release date: 2016-06-22, Last modification date: 2024-01-10)
Primary citationRollen, K.,Granzin, J.,Panwalkar, V.,Arinkin, V.,Rani, R.,Hartmann, R.,Krauss, U.,Jaeger, K.E.,Willbold, D.,Batra-Safferling, R.
Signaling States of a Short Blue-Light Photoreceptor Protein PpSB1-LOV Revealed from Crystal Structures and Solution NMR Spectroscopy.
J.Mol.Biol., 428:3721-3736, 2016
Cited by
PubMed Abstract: Light-Oxygen-Voltage (LOV) domains represent the photo-responsive domains of various blue-light photoreceptor proteins and are widely distributed in plants, algae, fungi, and bacteria. Here, we report the dark-state crystal structure of PpSB1-LOV, a slow-reverting short LOV protein from Pseudomonas putida that is remarkably different from our previously published "fully light-adapted" structure [1]. A direct comparison of the two structures provides insight into the light-activated signaling mechanism. Major structural differences involve a~11Å movement of the C terminus in helix Jα, ~4Å movement of Hβ-Iβ loop, disruption of hydrogen bonds in the dimer interface, and a~29° rotation of chain-B relative to chain-A as compared to the light-state dimer. Both crystal structures and solution NMR data are suggestive of the key roles of a conserved glutamine Q116 and the N-cap region consisting of A'α-Aβ loop and the A'α helix in controlling the light-activated conformational changes. The activation mechanism proposed here for the PpSB1-LOV supports a rotary switch mechanism and provides insights into the signal propagation mechanism in naturally existing and artificial LOV-based, two-component systems and regulators.
PubMed: 27291287
DOI: 10.1016/j.jmb.2016.05.027
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.67 Å)
Structure validation

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数据于2025-06-25公开中

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