Electrostatic free energies in translational GTPases: Classic allostery and the rest

• Published in: Biochimica et biophysica acta Vol. 1850; no. 5; pp. 1006 - 1016
• Main Authors: Simonson, Thomas, Aleksandrov, Alexey, Satpati, Priyadarshi
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 01.05.2015; Elsevier
• Subjects: adenosinetriphosphatase; Allosteric Regulation; Archaeal Proteins - chemistry; Archaeal Proteins - metabolism; Biochemistry, Molecular Biology; computational chemistry; continuum electrostatics; Energy Transfer; Enzyme Activation; genetic code; Gibbs free energy; GTP Phosphohydrolases - chemistry; GTP Phosphohydrolases - metabolism; Guanosine Diphosphate - chemistry; Guanosine Diphosphate - metabolism; guanosine triphosphate; Guanosine Triphosphate - chemistry; Guanosine Triphosphate - metabolism; guanosinetriphosphatase; induced fit; ions; Life Sciences; Ligands; magnesium; Magnesium - chemistry; molecular dynamics; Molecular Dynamics Simulation; Molecular recognition; Peptide Initiation Factors - chemistry; Peptide Initiation Factors - metabolism; Protein Conformation; Static Electricity; Structure-Activity Relationship; Thermodynamics; translation (genetics); IS/OS; MDFE; PBFE; MD; ATP/GTP; Molecular recognition; induced fit; molecular dynamics; computational chemistry; aIF2/aIF5B; continuum electrostatics

GTPases typically switch between an inactive, OFF conformation and an active, ON conformation when a GDP ligand is replaced by GTP. Their ON/OFF populations and activity thus depend on the stabilities of four protein complexes, two apo-protein forms, and GTP/GDP in solution. A complete characterizat...