6HZK

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

6HZK の概要

• エントリーDOI: 10.2210/pdb6hzk/pdb
• 分子名称: Phosphoribulokinase (2 entities in total)
• 機能のキーワード: phosphoribulokinase, calvin cycle, transferase
• 由来する生物種: Synechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1) (Anacystis nidulans)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 75521.50

構造登録者

Wilson, R.H.,Bracher, A.,Hartl, F.U.,Hayer-Hartl, M. (登録日: 2018-10-23, 公開日: 2019-03-27, 最終更新日: 2024-10-09)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.4 Å)