Literature DB >> 12781764

Structural framework for catalysis and regulation in ribulose-1,5-bisphosphate carboxylase/oxygenase.

Inger Andersson1, Thomas C Taylor.   

Abstract

Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) is the enzyme assimilating CO2 in biology. Despite serious efforts, using many different methods, a detailed understanding of activity and regulation in Rubisco still eludes us. New results in X-ray crystallography may provide a structural framework on which to base experimental approaches for more detailed analyses of the function of Rubisco at the molecular level. This article gives a critical review of the field and summarizes recent results from structural studies of Rubisco.

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Year:  2003        PMID: 12781764     DOI: 10.1016/s0003-9861(03)00164-4

Source DB:  PubMed          Journal:  Arch Biochem Biophys        ISSN: 0003-9861            Impact factor:   4.013


  19 in total

1.  The catalytic and conformational cycle of Aquifex aeolicus KDO8P synthase: role of the L7 loop.

Authors:  Xingjue Xu; Fathima Kona; Jian Wang; Jinshuang Lu; Timothy Stemmler; Domenico L Gatti
Journal:  Biochemistry       Date:  2005-09-20       Impact factor: 3.162

2.  High heterogeneity within the ribosomal proteins of the Arabidopsis thaliana 80S ribosome.

Authors:  Patrick Giavalisco; Daniel Wilson; Thomas Kreitler; Hans Lehrach; Joachim Klose; Johan Gobom; Paola Fucini
Journal:  Plant Mol Biol       Date:  2005-03       Impact factor: 4.076

Review 3.  Function, structure, and evolution of the RubisCO-like proteins and their RubisCO homologs.

Authors:  F Robert Tabita; Thomas E Hanson; Huiying Li; Sriram Satagopan; Jaya Singh; Sum Chan
Journal:  Microbiol Mol Biol Rev       Date:  2007-12       Impact factor: 11.056

4.  Coupled chaperone action in folding and assembly of hexadecameric Rubisco.

Authors:  Cuimin Liu; Anna L Young; Amanda Starling-Windhof; Andreas Bracher; Sandra Saschenbrecker; Bharathi Vasudeva Rao; Karnam Vasudeva Rao; Otto Berninghausen; Thorsten Mielke; F Ulrich Hartl; Roland Beckmann; Manajit Hayer-Hartl
Journal:  Nature       Date:  2010-01-14       Impact factor: 49.962

5.  Structure of the RuBisCO chaperone RbcX from the thermophilic cyanobacterium Thermosynechococcus elongatus.

Authors:  Miroslaw Tarnawski; Szymon Krzywda; Wojciech Bialek; Mariusz Jaskolski; Andrzej Szczepaniak
Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun       Date:  2011-07-13

6.  Crystal structure of a chaperone-bound assembly intermediate of form I Rubisco.

Authors:  Andreas Bracher; Amanda Starling-Windhof; F Ulrich Hartl; Manajit Hayer-Hartl
Journal:  Nat Struct Mol Biol       Date:  2011-07-17       Impact factor: 15.369

7.  Opposing effects of folding and assembly chaperones on evolvability of Rubisco.

Authors:  Paulo Durão; Harald Aigner; Péter Nagy; Oliver Mueller-Cajar; F Ulrich Hartl; Manajit Hayer-Hartl
Journal:  Nat Chem Biol       Date:  2015-01-05       Impact factor: 15.040

8.  Substitutions at the opening of the Rubisco central solvent channel affect holoenzyme stability and CO2/O 2 specificity but not activation by Rubisco activase.

Authors:  M Gloria Esquivel; Todor Genkov; Ana S Nogueira; Michael E Salvucci; Robert J Spreitzer
Journal:  Photosynth Res       Date:  2013-09-07       Impact factor: 3.573

9.  Rational 'correction' of the amino-acid sequence of RbcX protein from the thermophilic cyanobacterium Thermosynechococcus elongatus dramatically improves crystallization.

Authors:  Miroslaw Tarnawski; Szymon Krzywda; Andrzej Szczepaniak; Mariusz Jaskolski
Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun       Date:  2008-08-29

Review 10.  Directing the evolution of Rubisco and Rubisco activase: first impressions of a new tool for photosynthesis research.

Authors:  Oliver Mueller-Cajar; Spencer M Whitney
Journal:  Photosynth Res       Date:  2008-07-15       Impact factor: 3.573

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