3qv1

Crystal structure of the binary complex of photosyntetic A4 glyceraldehyde 3-phosphate dehydrogenase (GAPDH) with cp12-2, both from Arabidopsis thaliana.

spinqualitylabelsall models 3qv1, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3qv1 is a 9 chain structure with sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2Å Ligands: EDO, NAD, PEG, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function CP122_ARATH Acts as a linker essential in the assembly of a core complex of PRK/GAPDH. Coordinates the reversible inactivation of chloroplast enzymes GAPDH and PRK during darkness in photosynthetic tissues. Publication Abstract from PubMed Carbon assimilation in plants is regulated by the reduction of specific protein disulfides by light and their re-oxidation in the dark. The redox switch CP12 is an intrinsically disordered protein that can form two disulfide bridges. In the dark oxidized CP12 forms an inactive supramolecular complex with glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and phosphoribulokinase, two enzymes of the carbon assimilation cycle. Here we show that binding of CP12 to GAPDH, the first step of ternary complex formation, follows an integrated mechanism that combines conformational selection with induced folding steps. Initially, a CP12 conformation characterized by a circular structural motif including the C-terminal disulfide is selected by GAPDH. Subsequently, the induced folding of the flexible C-terminal tail of CP12 in the active site of GAPDH stabilizes the binary complex. Formation of several hydrogen bonds compensates the entropic cost of CP12 fixation and terminates the interaction mechanism that contributes to carbon assimilation control. Conformational Selection and Folding-upon-binding of Intrinsically Disordered Protein CP12 Regulate Photosynthetic Enzymes Assembly.,Fermani S, Trivelli X, Sparla F, Thumiger A, Calvaresi M, Marri L, Falini G, Zerbetto F, Trost P J Biol Chem. 2012 Jun 15;287(25):21372-83. Epub 2012 Apr 18. PMID:22514274 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Glyceraldehyde-3-phosphate dehydrogenase 3D structures

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