 |
PDBsum entry 2ddn
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Photosynthesis
|
PDB id
|
|
|
|
2ddn
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
| |
|
|
J Mol Graph Model
25:186-195
(2006)
|
|
PubMed id:
|
|
|
|
|
|
| |
|
Construction of a 3D model of CP12, a protein linker.
|
|
F.Gardebien,
R.R.Thangudu,
B.Gontero,
B.Offmann.
|
|
|
|
|
| |
ABSTRACT
|
|
|
|
| |
|
|
The chloroplast protein CP12 is known to play a leading role in a complex
formation with the enzymes GAPDH and PRK. As a preliminary step towards the
understanding of the complex formation mechanism and the exact role of this
protein linker, a comparative modelling of the CP12 protein of the green alga
Chlamydomonas reinhardtii was performed. Because of the very few structural
information and poor template similarities, the derivation of the model
consisted in an iterative trial-and-error procedure using the comparative
modelling program MODELLER, the following three structure validation programs
PROCHECK, PROSA, and WHATIF, and molecular mechanics energy refinement of the
model using the program CHARMM. The analysis of the final model reveals a
scaffold of key residues that is believed to be essential in the folding
mechanism and that coincides with the residues conserved throughout the CP12
family. Our results suggest that this protein is a typical disordered protein.
Finally, the various mechanisms by which the CP12 protein can self-interact or
binds to other enzymes are discussed in light of its modelled structure and
characteristics.
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
 |
 |
|
Literature references that cite this PDB file's key reference
|
|
|
| |
PubMed id
|
|
Reference
|
|
|
|
|
|
R.Groben,
D.Kaloudas,
C.A.Raines,
B.Offmann,
S.C.Maberly,
and
B.Gontero
(2010).
Comparative sequence analysis of CP12, a small protein involved in the formation of a Calvin cycle complex in photosynthetic organisms.
|
| |
Photosynth Res,
103,
183-194.
|
|
|
|
|
|
|
J.Erales,
S.Lignon,
and
B.Gontero
(2009).
CP12 from Chlamydomonas reinhardtii, a Permanent Specific "Chaperone-like" Protein of Glyceraldehyde-3-phosphate Dehydrogenase.
|
| |
J Biol Chem,
284,
12735-12744.
|
|
|
|
|
|
|
J.Erales,
L.Avilan,
S.Lebreton,
and
B.Gontero
(2008).
Exploring CP12 binding proteins revealed aldolase as a new partner for the phosphoribulokinase/glyceraldehyde 3-phosphate dehydrogenase/CP12 complex--purification and kinetic characterization of this enzyme from Chlamydomonas reinhardtii.
|
| |
FEBS J,
275,
1248-1259.
|
|
|
|
|
|
|
L.Marri,
P.Trost,
X.Trivelli,
L.Gonnelli,
P.Pupillo,
and
F.Sparla
(2008).
Spontaneous Assembly of Photosynthetic Supramolecular Complexes as Mediated by the Intrinsically Unstructured Protein CP12.
|
| |
J Biol Chem,
283,
1831-1838.
|
|
|
|
|
|
|
P.Singh,
D.Kaloudas,
and
C.A.Raines
(2008).
Expression analysis of the Arabidopsis CP12 gene family suggests novel roles for these proteins in roots and floral tissues.
|
| |
J Exp Bot,
59,
3975-3985.
|
|
|
|
|
|
|
P.Trost,
S.Fermani,
L.Marri,
M.Zaffagnini,
G.Falini,
S.Scagliarini,
P.Pupillo,
and
F.Sparla
(2006).
Thioredoxin-dependent regulation of photosynthetic glyceraldehyde-3-phosphate dehydrogenase: autonomous vs. CP12-dependent mechanisms.
|
| |
Photosynth Res,
89,
263-275.
|
|
|
|
|
|
|
S.Lebreton,
S.Andreescu,
E.Graciet,
and
B.Gontero
(2006).
Mapping of the interaction site of CP12 with glyceraldehyde-3-phosphate dehydrogenase from Chlamydomonas reinhardtii. Functional consequences for glyceraldehyde-3-phosphate dehydrogenase.
|
| |
FEBS J,
273,
3358-3369.
|
|
|
|
|
|
The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
|
|
Links
