Unravelling the shape and structural assembly of the photosynthetic GAPDH-CP12-PRK complex from Arabidopsis thaliana by small-angle X-ray scattering analysis.
Acta Crystallogr D Biol Crystallogr
; 71(Pt 12): 2372-85, 2015 Dec 01.
Article
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| MEDLINE
| ID: mdl-26627646
ABSTRACT
Oxygenic photosynthetic organisms produce sugars through the Calvin-Benson cycle, a metabolism that is tightly linked to the light reactions of photosynthesis and is regulated by different mechanisms, including the formation of protein complexes. Two enzymes of the cycle, glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and phosphoribulokinase (PRK), form a supramolecular complex with the regulatory protein CP12 with the formula (GAPDH-CP122-PRK)2, in which both enzyme activities are transiently inhibited during the night. Small-angle X-ray scattering analysis performed on both the GAPDH-CP12-PRK complex and its components, GAPDH-CP12 and PRK, from Arabidopsis thaliana showed that (i) PRK has an elongated, bent and screwed shape, (ii) the oxidized N-terminal region of CP12 that is not embedded in the GAPDH-CP12 complex prefers a compact conformation and (iii) the interaction of PRK with the N-terminal region of CP12 favours the approach of two GAPDH tetramers. The interaction between the GAPDH tetramers may contribute to the overall stabilization of the GAPDH-CP12-PRK complex, the structure of which is presented here for the first time.
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Bases de datos:
MEDLINE
Asunto principal:
Fotosíntesis
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Proteínas Portadoras
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Arabidopsis
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Fosfotransferasas (Aceptor de Grupo Alcohol)
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Gliceraldehído-3-Fosfato Deshidrogenasa (Fosforilante)
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Proteínas de Arabidopsis
Idioma:
En
Revista:
Acta Crystallogr D Biol Crystallogr
Año:
2015
Tipo del documento:
Article
País de afiliación:
Italia