Localization | Comment | Organism | GeneOntology No. | Textmining |
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Organism | UniProt | Comment | Textmining |
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Thermosynechococcus vestitus | P0A405 AND P0A407 AND P0A415 | genes psaA, psaB, and PsaC | - |
Subunits | Comment | Organism |
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monomer | inside the trimer, subunits PsaL, PsaI and PsaM (5 alpha-helices in total) are located in the center of the trimerization domain of PSI, thereby forming most of the contacts between the monomers | Thermosynechococcus vestitus |
trimer | inside the trimer, subunits PsaL, PsaI and PsaM (5 alpha-helices in total) are located in the center of the trimerization domain of PSI, thereby forming most of the contacts between the monomers | Thermosynechococcus vestitus |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
20 | 100 | analysis of thermostability of oligomeric PSI complexes. The thermal profile of the spectral shift of alpha-helices bands confirms the same two temperature intervals for PSI monomers and only one interval for trimers. Spectra at 20-100°C show distinct changes in the Amide I region of PSI complexes as a function of the rising temperature. Absorbance at the Amide I maximum of PSI monomers, gradually drops in two temperature intervals, i.e. 60-75°C and 80-90°C. In contrast, absorbance at the Amide I maximum of PSI trimers drops only in one temperature interval 80-95°C. Spectral changes of PSI trimers and monomers heated up to 100°C are irreversible due to protein denaturation and non-specific aggregation of complexes leading to new absorption bands. Thermal denaturation profiles, detailed overview, The enzyme shows denaturation at the monomer-monomer-interface at over 60°C, and denaturation/aggregation at the trimer-lipid interface at over 80°C. Oligomerization is one strategy to increase thermostability of PSI complexes | Thermosynechococcus vestitus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
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7.4 | - |
assay at | Thermosynechococcus vestitus |