The transition between the open and closed states of rubisco is triggered by the inter-phosphate distance of the bound bisphosphate
- 19 May 2000
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 298 (5), 903-916
- https://doi.org/10.1006/jmbi.2000.3724
Abstract
No abstract availableKeywords
This publication has 22 references indexed in Scilit:
- Mechanism of Rubisco: The Carbamate as General BaseChemical Reviews, 1998
- Side Reactions Catalyzed by Ribulose-bisphosphate Carboxylase in the Presence and Absence of Small SubunitsPublished by Elsevier ,1997
- Checking your imagination: applications of the free R valueStructure, 1996
- Large Structures at High Resolution: The 1.6 Å Crystal Structure of Spinach Ribulose-1,5- Bisphosphate Carboxylase/Oxygenase Complexed with 2-Carboxyarabinitol BisphosphateJournal of Molecular Biology, 1996
- STRUCTURE, FUNCTION, REGULATION, AND ASSEMBLY OF D-RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE/OXYGENASEAnnual Review of Biochemistry, 1994
- Structure of an effector-induced inactivated state of ribulose 1,5-bisphosphate carboxylase/oxygenase: the binary complex between enzyme and xylulose 1,5-bisphosphateStructure, 1994
- Improved methods for building protein models in electron density maps and the location of errors in these modelsActa Crystallographica Section A Foundations of Crystallography, 1991
- Crystallographic analysis of ribulose 1,5-bisphosphate carboxylase from spinach at 2·4 Å resolutionJournal of Molecular Biology, 1990
- On the three-dimensional structure and catalytic mechanism of triose phosphate isomerasePhilosophical Transactions of the Royal Society of London. B, Biological Sciences, 1981
- Interaction of sugar phosphates with the catalytic site of ribulose-1,5-bisphosphate carboxylaseBiochemistry, 1981