A bisubstrate analog induces unexpected conformational changes in phosphoglycerate kinase from Trypanosoma brucei
- 1 June 1998
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 279 (5) , 1137-1148
- https://doi.org/10.1006/jmbi.1998.1835
Abstract
No abstract availableKeywords
This publication has 26 references indexed in Scilit:
- Crystal Structures of Substrates and Products Bound to the Phosphoglycerate Kinase Active Site Reveal the Catalytic MechanismBiochemistry, 1998
- The importance of dynamic light scattering in obtaining multiple crystal forms of trypanosoma brucei PGKProtein Science, 1998
- Closed structure of phosphoglycerate kinase from Thermotoga maritima reveals the catalytic mechanism and determinants of thermal stabilityStructure, 1997
- Synergistic effects of substrate-induced conformational changes in phosphoglycerate kinase activationNature, 1997
- Conformational changes in yeast phosphoglycerate kinase upon substrate bindingBiophysical Chemistry, 1994
- The CCP4 suite: programs for protein crystallographyActa Crystallographica Section D-Biological Crystallography, 1994
- Structure of the ADP complex of the 3-phosphoglycerate kinase from Bacillus stearothermophilus at 1.65 ÅActa Crystallographica Section D-Biological Crystallography, 1994
- Crystal structure of the binary complex of pig muscle phosphoglycerate kinase and its substrate 3‐phospho‐D‐glycerateProteins-Structure Function and Bioinformatics, 1992
- 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
- Sequence, structure and activity of phosphoglycerate kinase: a possible hinge-bending enzymeNature, 1979