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  Crystal structure of phosphoribulokinase from Synechococcus sp. strain PCC 6301

Wilson, R. H., Hayer-Hartl, M., & Bracher, A. (2019). Crystal structure of phosphoribulokinase from Synechococcus sp. strain PCC 6301. Acta Crystallographica Section F: Structural Biology Communications, 75(4), 278-289. doi:10.1107/S2053230X19002693.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0003-DD1E-4 Version Permalink: http://hdl.handle.net/21.11116/0000-0003-DD1F-3
Genre: Journal Article

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 Creators:
Wilson, Robert H.1, Author              
Hayer-Hartl, Manajit1, Author              
Bracher, Andreas2, Author              
Affiliations:
1Hayer-Hartl, Manajit / Chaperonin-assisted Protein Folding, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565153              
2Hartl, Franz-Ulrich / Cellular Biochemistry, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565152              

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Free keywords: GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE; CHLAMYDOMONAS-REINHARDTII; MULTIENZYME COMPLEXES; INFORMATION-TRANSFER; PROTEIN; MODEL; INTERFACE; RESIDUES; ROLES; SITEBiochemistry & Molecular Biology; Biophysics; Crystallography; phosphoribulokinase; Calvin-Benson-Bassham cycle; photosynthesis; dark reaction; redox regulation; transferases;
 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 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.

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Language(s): eng - English
 Dates: 2019
 Publication Status: Published in print
 Pages: 12
 Publishing info: -
 Table of Contents: -
 Rev. Method: -
 Identifiers: ISI: 000463600400009
DOI: 10.1107/S2053230X19002693
 Degree: -

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Title: Acta Crystallographica Section F: Structural Biology Communications
Source Genre: Journal
 Creator(s):
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Publ. Info: Blackwell Publishing Limited
Pages: - Volume / Issue: 75 (4) Sequence Number: - Start / End Page: 278 - 289 Identifier: ISSN: 1744-3091
CoNE: https://pure.mpg.de/cone/journals/resource/1000000000017210_1