6HZK
Crystal structure of redox-inhibited phosphoribulokinase from Synechococcus sp. (strain PCC 6301)
Summary for 6HZK
| Entry DOI | 10.2210/pdb6hzk/pdb |
| Descriptor | Phosphoribulokinase (2 entities in total) |
| Functional Keywords | phosphoribulokinase, calvin cycle, transferase |
| Biological source | Synechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1) (Anacystis nidulans) |
| Total number of polymer chains | 2 |
| Total formula weight | 75521.50 |
| Authors | Wilson, R.H.,Bracher, A.,Hartl, F.U.,Hayer-Hartl, M. (deposition date: 2018-10-23, release date: 2019-03-27, Last modification date: 2024-10-09) |
| Primary citation | Wilson, R.H.,Hayer-Hartl, M.,Bracher, A. Crystal structure of phosphoribulokinase from Synechococcus sp. strain PCC 6301. Acta Crystallogr.,Sect.F, 75:278-289, 2019 Cited by PubMed Abstract: 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 α/β-fold with an 18-stranded β-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. PubMed: 30950829DOI: 10.1107/S2053230X19002693 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
Download full validation report
