Structural highlights
Publication Abstract from PubMed
Phosphoribulokinase (PRK) catalyses the ATP-dependent phosphorylation of ribulose 5-phosphate to give ribulose 1,5-bisphosphate. Regulation of this reaction in response to light controls carbon fixation during photosynthesis. Here, the crystal structure of PRK from the cyanobacterium Synechococcus sp. strain PCC 6301 is presented. The enzyme is dimeric and has an alpha/beta-fold with an 18-stranded beta-sheet at its core. Interestingly, a disulfide bond is found between Cys40 and the P-loop residue Cys18, revealing the structural basis for the redox inactivation of PRK activity. A second disulfide bond appears to rigidify the dimer interface and may thereby contribute to regulation by the adaptor protein CP12 and glyceraldehyde-3-phosphate dehydrogenase.
Crystal structure of phosphoribulokinase from Synechococcus sp. strain PCC 6301.,Wilson RH, Hayer-Hartl M, Bracher A Acta Crystallogr F Struct Biol Commun. 2019 Apr 1;75(Pt 4):278-289. doi:, 10.1107/S2053230X19002693. Epub 2019 Apr 2. PMID:30950829[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Wilson RH, Hayer-Hartl M, Bracher A. Crystal structure of phosphoribulokinase from Synechococcus sp. strain PCC 6301. Acta Crystallogr F Struct Biol Commun. 2019 Apr 1;75(Pt 4):278-289. doi:, 10.1107/S2053230X19002693. Epub 2019 Apr 2. PMID:30950829 doi:http://dx.doi.org/10.1107/S2053230X19002693
