Structural Investigation of PsbO from Plant and Cyanobacterial Photosystem II

Slowik, Daria; Rossmann, Maxim; Konarev, Petr V.; Irrgang, Klaus−Dieter

doi:10.1016/j.jmb.2011.01.013

Cited by 15 publications

(8 citation statements)

References 67 publications

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“…High sequence identity of PsbO between Thermo synechococcus and a higher plant (about 45%) disclosed a homologous model for plant PsbO [40]. X-ray scattering data revealed that PsbO from spinach and cyanobacteria have similar structures and oxygen-evolving rates [52].…”

Section: Psbomentioning

confidence: 99%

Photosystem II Extrinsic Proteins and Their Putative Role in Abiotic Stress Tolerance in Higher Plants

Sasi

Venkatesh

Daneshi

et al. 2018

Plants

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Abiotic stress remains one of the major challenges in managing and preventing crop loss. Photosystem II (PSII), being the most susceptible component of the photosynthetic machinery, has been studied in great detail over many years. However, much of the emphasis has been placed on intrinsic proteins, particularly with respect to their involvement in the repair of PSII-associated damage. PSII extrinsic proteins include PsbO, PsbP, PsbQ, and PsbR in higher plants, and these are required for oxygen evolution under physiological conditions. Changes in extrinsic protein expression have been reported to either drastically change PSII efficiency or change the PSII repair system. This review discusses the functional role of these proteins in plants and indicates potential areas of further study concerning these proteins.

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Section: Psbomentioning

confidence: 99%

Photosystem II Extrinsic Proteins and Their Putative Role in Abiotic Stress Tolerance in Higher Plants

Sasi

Venkatesh

Daneshi

et al. 2018

Plants

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“…SANS is also a powerful experimental tool for determining the solution structures of the assemblies of pigment–protein complexes − or of complexes undergoing structural changes upon external triggers . Furthermore, the solution structures of the major light-harvesting complex LHC II of green plants, PsbO from cyanobacterial photosystem II, the bacterial light-harvesting complex LH2 at physiological temperatures, and PS I trimers , were also determined by SANS and SAXS measurements. The advantage of both methods is also that free micelles in the ßDM–dPSIIcc solution can be determined before crystallization.…”

Section: Introductionmentioning

confidence: 99%

Solution Structure of the Detergent–Photosystem II Core Complex Investigated by Small-Angle Scattering Techniques

et al. 2020

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Albeit achieving the X-ray diffraction structure of dimeric photosystem II core complexes (dPSIIcc) at the atomic resolution, the nature of the detergent belt surrounding dPSIIcc remains ambiguous. Therefore, the solution structure of the whole detergent−protein complex of dPSIIcc of Thermosynechococcus elongatus (T. elongatus) solubilized in n-dodecyl-ß-D-maltoside (ßDM) was investigated by a combination of small-angle X-ray scattering (SAXS) and small-angle neutron scattering (SANS) with contrast variation. First, the structure of dPSIIcc was studied separately in SANS experiments using a contrast of 5% D 2 O. Guinier analysis reveals that the dPSIIcc solution is virtually free of aggregation in the studied concentration range of 2−10 mg/mL dPSIIcc, and characterized by a radius of gyration of 62 Å. A structure reconstitution shows that dPSIIcc in buffer solution widely retains the crystal structure reported by Xray free electron laser studies at room temperature with a slight expansion of the entire protein. Additional SANS experiments on dPSIIcc samples in a buffer solution containing 75% D 2 O provide information about the size and shape of the whole detergent− dPSIIcc. The maximum position of P(r) function increases to 68 Å, i.e., it is about 6 Å larger than that of dPSIIcc only, thus indicating the presence of an additional structure. Thus, it can be concluded that dPSIIcc is surrounded by a monomolecular belt of detergent molecules under appropriate solubilization conditions. The homogeneity of the ßDM−dPSIIcc solutions was also verified using dynamic light scattering. Complementary SAXS experiments indicate the presence of unbound detergent micelles by a separate peak consistent with a spherical shape possessing a radius of about 40 Å. The latter structure also contributes to the SANS data but rather broadens the SANS curve artificially. Without the simultaneous inspection of SANS and SAXS data, this effect may lead to an apparent underestimation of the size of the PS II−detergent complex. The formation of larger unbound detergent aggregates in solution prior to crystallization may have a significant effect on the crystal formation or quality of the ßDM−dPSIIcc.

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“…Full-length PsbO has previously been produced in Escherichia coli , but its production was shown to be crucially dependent on the formation of the C19–C44 disulfide bond, which staples the N-terminus to the β-barrel . Previous strategies included periplasmic targeting, ,, an N-terminal E. coli thioredoxin (trxA) tag, , refolding, and the use of a disulfide-competent E. coli strain . The thioredoxin fusion has the advantage of robust expression of the fusion partner in E. coli …”

Section: Methodsmentioning

confidence: 99%

“…β-barrel. 32 Previous strategies included periplasmic targeting, 31,33,34 an N-terminal E. coli thioredoxin (trxA) tag, 32,35 refolding, 36 and the use of a disulfide-competent E. coli strain. 37 The thioredoxin fusion has the advantage of robust expression of the fusion partner in E. coli.…”

Section: ■ Experimental Proceduresmentioning

confidence: 99%

Crystallographic and Computational Analysis of the Barrel Part of the PsbO Protein of Photosystem II: Carboxylate–Water Clusters as Putative Proton Transfer Relays and Structural Switches

et al. 2016

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In all organisms that employ oxygenic photosynthesis, the membrane-extrinsic PsbO protein is a functionally important component of photosystem II. To study the previously proposed proton antenna function of carboxylate clusters at the protein-water interface, we combined crystallography and simulations of a truncated cyanobacterial (Thermosynechococcus elongatus) PsbO without peripheral loops. We expressed the PsbO β-barrel heterologously and determined crystal structures at resolutions of 1.15-1.5 Å at 100 K at various pH values and at 297 K and pH 6. (1) Approximately half of the 177 surface waters identified at 100 K are resolved at 297 K, suggesting significant occupancy of specific water sites at room temperature, and loss of resolvable occupancy for other sites. (2) Within a loop region specific to cyanobacterial PsbO, three residues and four waters coordinating a calcium ion are well ordered even at 297 K; the ligation differs for manganese. (3) The crystal structures show water-carboxylate clusters that could facilitate fast Grotthus-type proton transfer along the protein surface and/or store protons. (4) Two carboxylate side chains, which are part of a structural motif interrupting two β-strands and connecting PsbO to photosystem II, are within hydrogen bonding distance at pH 6 (100 K). Simulations indicate coupling between protein structure and carboxylate protonation. The crystal structure determined at 100 K and pH 10 indicates broken hydrogen bonding between the carboxylates and local structural change. At pH 6 and 297 K, both conformations were present in the crystal, suggesting conformational dynamics in the functionally relevant pH regime. Taken together, crystallography and molecular dynamics underline a possible mechanism for pH-dependent structural switching.

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Structural Investigation of PsbO from Plant and Cyanobacterial Photosystem II

Cited by 15 publications

References 67 publications

Photosystem II Extrinsic Proteins and Their Putative Role in Abiotic Stress Tolerance in Higher Plants

Photosystem II Extrinsic Proteins and Their Putative Role in Abiotic Stress Tolerance in Higher Plants

Solution Structure of the Detergent–Photosystem II Core Complex Investigated by Small-Angle Scattering Techniques

Crystallographic and Computational Analysis of the Barrel Part of the PsbO Protein of Photosystem II: Carboxylate–Water Clusters as Putative Proton Transfer Relays and Structural Switches

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