2LJ9

Partial 3d structure of the c-terminal part of the free arabidopsis thaliana cp12-2 in its oxidized form

Summary for 2LJ9

• Entry DOI: 10.2210/pdb2lj9/pdb
• NMR Information: BMRB: 17926
• Descriptor: CP12 domain-containing protein 2 (1 entity in total)
• Functional Keywords: helix, protein binding, intrinsically disordered protein
• Biological source: Arabidopsis thaliana (mouse-ear cress,thale-cress)
• Cellular location: Plastid, chloroplast: Q9LZP9
• Total number of polymer chains: 1
• Total formula weight: 10643.46

Authors

Trivelli, X.,Sparla, F.,Marri, L.,Trost, P. (deposition date: 2011-09-09, release date: 2012-04-25, Last modification date: 2024-10-30)

Primary citation

Fermani, S.,Trivelli, X.,Sparla, F.,Thumiger, A.,Calvaresi, M.,Marri, L.,Falini, G.,Zerbetto, F.,Trost, P.
Conformational Selection and Folding-upon-binding of Intrinsically Disordered Protein CP12 Regulate Photosynthetic Enzymes Assembly.
J.Biol.Chem., 287:21372-21383, 2012

PubMed Abstract: 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.

PubMed: 22514274
DOI: 10.1074/jbc.M112.350355

Experimental method

SOLUTION NMR