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Literature summary for 1.97.1.12 extracted from

  • Mazor, Y.; Borovikova, A.; Caspy, I.; Nelson, N.
    Structure of the plant photosystem I supercomplex at 2.6 A resolution (2017), Nat. Plants, 3, 17014 .
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
purified plant photosystem I supercomplex including light-harvesting complex I, sitting drop vapour diffusion technique, mixing of 0.006-0.008 ml of PSI protein solution with an equal volume of reservoir solution containing 50 mM di-potassium phosphate, 50 mM Tris, pH 8, 12-17% PEG 400, 1% glycerol, 2 mM L-glutathione, and 0.03% octyl glucose neopentyl glycol, and equilibration against 0.5 ml of reservoir solution, 4°C, 1 month, X-ray diffraction structure determination and analysis at 2.6 A resolution, single-wavelength anomalous diffraction phasing of PSI-LHCI Pisum sativum

Localization

Localization Comment Organism GeneOntology No. Textmining
thylakoid membrane
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Pisum sativum 42651
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Organism

Organism UniProt Comment Textmining
Pisum sativum P17227 var. Kalvadon
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Purification (Commentary)

Purification (Comment) Organism
native enzyme complex from detergent-treated thylakoid membranes by two steps of anion exchange chromatography with elution through tetraethylammonium chloride followed by precipitation with PEG 6000 and PEG 1500, respectively Pisum sativum

Source Tissue

Source Tissue Comment Organism Textmining
leaf
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Pisum sativum
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Subunits

Subunits Comment Organism
More the crystal structure reveals the configuration of PsaK, a core subunit important for state transitions in plants, a conserved network of water molecules surrounding the electron transfer centres and an elaborate structure of lipids bridging PSI and its LHCI antenna. The structure of Psak suggests alternative conformations, overview Pisum sativum

Synonyms

Synonyms Comment Organism
PSI
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Pisum sativum

General Information

General Information Comment Organism
additional information lipid structure and enzyme complex structure analysis of photosystem I supercomplex including light-harvesting complex I, PSI-LHCI, overview. Foerster rate calculations reveal the importance of the luminal-side pigment junctions. Chlorophyll b molecules are coordinated by a mixture of polar and hydrophobic interactions Pisum sativum
physiological function photosystem I (PSI) is one of two large reaction centres responsible for converting light photons into the chemical energy needed to sustain life. In the thylakoid membranes of plants, PSI is found together with its integral light-harvesting antenna, light-harvesting complex I (LHCI), in a membrane supercomplex containing hundreds of light-harvesting pigments Pisum sativum