Structural highlights
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
In some cyanobacteria, the genes for the large and small subunits of the enzyme RuBisCO are separated on the bacterial chromosome by the insertion of a gene coding for a protein designated RbcX, which acts as a chaperone for RuBisCO. A recent structural study [Saschenbrecker et al. (2007), Cell, 129, 1189-1200] has shed light on the mechanism by which RbcX assists RuBisCO assembly. Here, the crystal structure of RbcX from another cyanobacterium, Synechocystis sp. PCC6803, is reported, revealing an unusually long protruding C-terminal helix, as well as a bound polyethylene glycol molecule in the protein substrate-binding site.
Structure of the RuBisCO chaperone RbcX from Synechocystis sp. PCC6803.,Tanaka S, Sawaya MR, Kerfeld CA, Yeates TO Acta Crystallogr D Biol Crystallogr. 2007 Oct;63(Pt 10):1109-12. Epub 2007, Sep 19. PMID:17881829[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Tanaka S, Sawaya MR, Kerfeld CA, Yeates TO. Structure of the RuBisCO chaperone RbcX from Synechocystis sp. PCC6803. Acta Crystallogr D Biol Crystallogr. 2007 Oct;63(Pt 10):1109-12. Epub 2007, Sep 19. PMID:17881829 doi:10.1107/S090744490704228X
