SASDDE9: Synechocystis fluorescence recovery protein FRPcc in the pre-oxid...

Basic information

• Entry: Database: SASBDB / ID: SASDDE9

Sample

Synechocystis fluorescence recovery protein FRPcc in the pre-oxidized state (CC mutant)

• Fluorescence recovery protein (protein), Synechocystis sp. (strain PCC 6803 / Kazusa)

• Function / homology: Fluorescence recovery protein / : / Photoprotection regulator fluorescence recovery protein / plasma membrane-derived thylakoid membrane / Fluorescence recovery protein
• Biological species: Synechocystis sp. (strain PCC 6803 / Kazusa) (bacteria)
• Citation: Journal: Nat Commun / Year: 2018; Title: OCP-FRP protein complex topologies suggest a mechanism for controlling high light tolerance in cyanobacteria.; Authors: Nikolai N Sluchanko / Yury B Slonimskiy / Evgeny A Shirshin / Marcus Moldenhauer / Thomas Friedrich / Eugene G Maksimov / ; Abstract: In cyanobacteria, high light photoactivates the orange carotenoid protein (OCP) that binds to antennae complexes, dissipating energy and preventing the destruction of the photosynthetic apparatus. At low light, OCP is efficiently deactivated by a poorly understood action of the dimeric fluorescence recovery protein (FRP). Here, we engineer FRP variants with defined oligomeric states and scrutinize their functional interaction with OCP. Complemented by disulfide trapping and chemical crosslinking, structural analysis in solution reveals the topology of metastable complexes of OCP and the FRP scaffold with different stoichiometries. Unable to tightly bind monomeric FRP, photoactivated OCP recruits dimeric FRP, which subsequently monomerizes giving 1:1 complexes. This could be facilitated by a transient OCP-2FRP-OCP complex formed via the two FRP head domains, significantly improving FRP efficiency at elevated OCP levels. By identifying key molecular interfaces, our findings may inspire the design of optically triggered systems transducing light signals into protein-protein interactions.

Contact author

• Nikolai Sluchanko (A.N. Bach Institute of Biochemistry, Moscow, Russia)

Models

• Model #2147: ; Type: mix / Radius of dummy atoms: 1.90 A / Chi-square value: 1.06 / P-value: 0.063614; Search similar-shape structures of this assembly by Omokage search (details)

Sample

• Sample: Name: Synechocystis fluorescence recovery protein FRPcc in the pre-oxidized state (CC mutant); Specimen concentration: 1.7 mg/ml
• Buffer: Name: 20 mM Tris 150 mM NaCl 3% glycerol / pH: 7.6

Entity #1175

Type: protein / Description: Fluorescence recovery protein / Formula weight: 14.09 / Num. of mol.: 2 / Source: Synechocystis sp. (strain PCC 6803 / Kazusa) / References: UniProt: P74103
Sequence:

MRGSHHHHHH TDPATMLQTA EAPWSQAETQ SAHALFRKAY QRELDGLCAT VQAQASQCTQ IDDLWKLHDF LSAKRHEIDG KYDDRQSVII FVFAQLLKEG LVQAEELTFL AADKQSKIKA LARL

Experimental information

• Beam: Instrument name: PETRA III EMBL P12 / City: Hamburg / 国: Germany / Type of source: X-ray synchrotron / Wavelength: 0.124 Å
• Detector: Name: Pilatus 2M

Scan

Title: Synechocystis fluorescence recovery protein FRPcc in the pre-oxidized state (CC mutant)
Measurement date: Sep 1, 2017 / Storage temperature: 20 °C / Cell temperature: 10 °C / Exposure time: 0.05 sec. / Number of frames: 20 / Unit: 1/nm /

	Min	Max
Q	0.1022	4.4376

Distance distribution function P(R)

Sofotware P(R): GNOM 5.0 / Number of points: 959 /

	Min	Max
Q	0.1022	2.74593
P(R) point	1	959
R	0	13

Result

Type of curve: single_conc /

	Experimental	Porod
MW	27.2 kDa	27.2 kDa
Volume	-	43.4 nm3

	P(R)	P(R) error	Guinier	Guinier error
Forward scattering, I0	0.01736	0.0001	0.017	-
Radius of gyration, Rg	3.131 nm	0.04	2.91 nm	0.09

	Min	Max
D	-	13
Guinier point	1	125