Structural highlights
Publication Abstract from PubMed
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.
Construction of a 3D model of CP12, a protein linker.,Gardebien F, Thangudu RR, Gontero B, Offmann B J Mol Graph Model. 2006 Oct;25(2):186-95. Epub 2006 Jan 19. PMID:16427344[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Gardebien F, Thangudu RR, Gontero B, Offmann B. Construction of a 3D model of CP12, a protein linker. J Mol Graph Model. 2006 Oct;25(2):186-95. Epub 2006 Jan 19. PMID:16427344 doi:10.1016/j.jmgm.2005.12.003
