| Structural highlights
3rvd is a 16 chain structure with sequence from Arath. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Ligands: | , |
| Related: | 3k2b, 3qv1 |
| Gene: | At3g26650, GAPA, MLJ15.4, MLJ15_5 (ARATH), At3g26650 (ARATH), T12C14_110, At3g62410 (ARATH) |
| Activity: | Glyceraldehyde-3-phosphate dehydrogenase (NADP(+)) (phosphorylating), with EC number 1.2.1.13 |
| Resources: | FirstGlance, OCA, RCSB, PDBsum |
Function
[G3PA1_ARATH] Involved in the photosynthetic reductive pentose phosphate pathway (Calvin-Benson cycle). Catalyzes the reduction of 1,3-diphosphoglycerate by NADPH (By similarity). [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.[1] [2]
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[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Marri L, Trost P, Pupillo P, Sparla F. Reconstitution and properties of the recombinant glyceraldehyde-3-phosphate dehydrogenase/CP12/phosphoribulokinase supramolecular complex of Arabidopsis. Plant Physiol. 2005 Nov;139(3):1433-43. Epub 2005 Oct 28. PMID:16258009 doi:10.1104/pp.105.068445
- ↑ Marri L, Pesaresi A, Valerio C, Lamba D, Pupillo P, Trost P, Sparla F. In vitro characterization of Arabidopsis CP12 isoforms reveals common biochemical and molecular properties. J Plant Physiol. 2010 Aug 15;167(12):939-50. doi: 10.1016/j.jplph.2010.02.008. PMID:20399532 doi:http://dx.doi.org/10.1016/j.jplph.2010.02.008
- ↑ 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. 2012 Jun 15;287(25):21372-83. Epub 2012 Apr 18. PMID:22514274 doi:10.1074/jbc.M112.350355
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