6HZL

Crystal structure of redox-inhibited phosphoribulokinase from Synechococcus sp. (strain PCC 6301), osmate derivative

Summary for 6HZL

• Entry DOI: 10.2210/pdb6hzl/pdb
• Descriptor: Phosphoribulokinase, OSMIUM ION (3 entities in total)
• Functional Keywords: phosphoribulokinase, calvin cycle, transferase
• Biological source: Synechococcus elongatus PCC 6301 (Anacystis nidulans)
• Total number of polymer chains: 2
• Total formula weight: 75901.96

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: 2024-11-13)

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

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: 30950829
DOI: 10.1107/S2053230X19002693

Experimental method

X-RAY DIFFRACTION (2.77 Å)