| General information | | DisProt: | DP00359 | | Name: | Calvin cycle protein CP12 | | Synonym(s): | CP12_CHLRE
Chloroplast protein 12
| | First appeared in release: | Release 3.0 (02/17/2006) | | UniProt: | A6Q0K5 | | UniGene: | | | SwissProt: | CP12_CHLRE | | TrEMBL: | | | NCBI (GI): | 158513810 | | Source organism: | Chlamydomonas reinhardtii | | Sequence length: | 80 | | Percent disordered: | 100% | | Homologues: | |
| Native sequence |
10 20 30 40 50 60
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SGQPAVDLNK KVQDAVKEAE DACAKGTSAD CAVAWDTVEE LSAAVSHKKD AVKADVTLTD - 60
PLEAFCKDAP DADECRVYED
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| Functional narrative |
CP12 is an 8.5-kDa nuclear-encoded chloroplast protein. It forms part of a core complex of two dimers of phosphoribulokinase (PRK), two tetramers of glyceraldehyde 3-phosphate dehydrogenase (GAPDH), and CP12. Oxidized CP12 modifies GAPDH kinetic properties and conformation and acts as a linker in the assembly of the GAPDH/CP12/PRK complex. In this complexed state these enzymes are inactivated, which provides a way to regulate their photosynthetic activities in the Calvin cycle. Acts as a linker essential in the assembly of a core complex of PRK/GAPDH.
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| Map of ordered and disordered regions |
Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.
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| Region 1 | | Type: | Disordered | | Name: | Reduced form | | Location: | 1 - 80 | | Length: | 80 | | Region sequence: |
SGQPAVDLNKKVQDAVKEAEDACAKGTSADCAVAWDTVEELSAAVSHKKDAVKADVTLTD
PLEAFCKDAPDADECRVYED | | Modification type: | Engineered
| | PDB: | 2DDN:A | | Structural/functional type: | Function arises via a disorder to order transition
| | Functional classes: | Molecular recognition scavengers
| | Functional subclasses: | Metal binding
| Detection methods:
- Nuclear magnetic resonance (NMR) (pH: 6; 2H2O (v/v) 10 %; NaCl 50 mM; NaH2PO4 50 mM)
- Circular dichroism (CD) spectroscopy, far-UV (pH: 6; Na2HPO4-NaH2PO4 10 mM)
| References:
- Delobel A, Graciet E, Andreescu S, Gontero B, Halgand F, Laprévote O. "Mass spectrometric analysis of the interactions between CP12, a chloroplast protein, and metal ions: a possible regulatory role within a PRK/GAPDH/CP12 complex." Rapid Commun Mass Spectrom. 2005; 19(22): 3379-88. PubMed: 16259044
- Gardebien F, Thangudu RR, Gontero B, Offmann B. "Construction of a 3D model of CP12, a protein linker." J Mol Graph Model. 2006; 25(2): 186-95. PubMed: 16427344
- Graciet E, Gans P, Wedel N, Lebreton S, Camadro JM, Gontero B. "The small protein CP12: a protein linker for supramolecular complex assembly." Biochemistry. 2003; 42(27): 8163-70. PubMed: 12846565
| Comments:The presence of copper cations catalyzes the re-formation of disulfide bonds in the reduced form of this protein. This in turn leads to the formation of the oxidized CP12, which can then bind a copper ion.
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| Region 2 | | Type: | Disordered | | Name: | Oxidized form | | Location: | 1 - 8 | | Length: | 8 | | Region sequence: |
SGQPAVDL | | Modification type: | Engineered
| | PDB: | 2DDN:A | | Structural/functional type: | Function arises from the disordered state
| | Functional classes: | Entropic chain
| | Functional subclasses: | Flexible linkers/spacers
| Detection methods:
- Circular dichroism (CD) spectroscopy, far-UV (pH: 6; Na2HPO4-NaH2PO4 10 mM)
- Nuclear magnetic resonance (NMR) (pH: 6; 2H2O (v/v) 10 %; NaCl 50 mM; NaH2PO4 50 mM)
| References:
- Delobel A, Graciet E, Andreescu S, Gontero B, Halgand F, Laprévote O. "Mass spectrometric analysis of the interactions between CP12, a chloroplast protein, and metal ions: a possible regulatory role within a PRK/GAPDH/CP12 complex." Rapid Commun Mass Spectrom. 2005; 19(22): 3379-88. PubMed: 16259044
- Gardebien F, Thangudu RR, Gontero B, Offmann B. "Construction of a 3D model of CP12, a protein linker." J Mol Graph Model. 2006; 25(2): 186-95. PubMed: 16427344
- Graciet E, Gans P, Wedel N, Lebreton S, Camadro JM, Gontero B. "The small protein CP12: a protein linker for supramolecular complex assembly." Biochemistry. 2003; 42(27): 8163-70. PubMed: 12846565
| Comments:
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| Region 3 | | Type: | Disordered - Molten Globule | | Name: | Oxidized form | | Location: | 53 - 65 | | Length: | 13 | | Region sequence: |
KADVTLTDPLEAF | | Modification type: | Engineered
| | PDB: | 2DDN:A | | Structural/functional type: | Function arises from the disordered state
| | Functional classes: | Molecular assembly
Entropic chain
| | Functional subclasses: | Flexible linkers/spacers
Protein-protein binding
| Detection methods:
- Circular dichroism (CD) spectroscopy, far-UV (pH: 6; Na2HPO4-NaH2PO4 10 mM)
- Nuclear magnetic resonance (NMR) (pH: 6; 2H2O (v/v) 10 %; NaCl 50 mM; NaH2PO4 50 mM)
| References:
- Delobel A, Graciet E, Andreescu S, Gontero B, Halgand F, Laprévote O. "Mass spectrometric analysis of the interactions between CP12, a chloroplast protein, and metal ions: a possible regulatory role within a PRK/GAPDH/CP12 complex." Rapid Commun Mass Spectrom. 2005; 19(22): 3379-88. PubMed: 16259044
- Gardebien F, Thangudu RR, Gontero B, Offmann B. "Construction of a 3D model of CP12, a protein linker." J Mol Graph Model. 2006; 25(2): 186-95. PubMed: 16427344
- Graciet E, Gans P, Wedel N, Lebreton S, Camadro JM, Gontero B. "The small protein CP12: a protein linker for supramolecular complex assembly." Biochemistry. 2003; 42(27): 8163-70. PubMed: 12846565
| Comments:
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| References |
- Graciet E, Lebreton S, Gontero B. "Emergence of new regulatory mechanisms in the Benson-Calvin pathway via protein-protein interactions: a glyceraldehyde-3-phosphate dehydrogenase/CP12/phosphoribulokinase complex." J Exp Bot. 2004; 55(400): 1245-54. PubMed: 15047759
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| Comments |
There is currently no database (i.e. SwissProt, etc.) reference for this protein.
While in the oxidized state, CP12 acts as a flexible linker between PRK and GAPDH. In the fully reduced and unstructured state, this function is lost.
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