作者: Johan Åqvist , Shina C. L. Kamerlin
DOI: 10.1021/BI501373G
关键词: Biochemistry 、 GTPase 、 Conformational change 、 Biophysics 、 Protein biosynthesis 、 GTP' 、 Histidine 、 Ribosome 、 Large ribosomal subunit 、 Enzyme 、 Biology
摘要: The translational GTPases hydrolyze GTP on the ribosome at several stages of protein synthesis cycle. Because strong conservation their catalytic center, these enzymes are expected to operate through a universal hydrolysis mechanism, in which critical histidine residue together with sarcin–ricin loop large ribosomal subunit is necessary for GTPase activation. Here we examine different possible pathways by EF-Tu extensive computer simulations. We show that conformational change peptide plane preceding this has decisive effect energetics reaction. This transition was predicted earlier us and recently been confirmed experimentally. It found promote early proton transfer from water γ-phosphate group GTP, followed nucleophilic attack hydroxide ion. calculated reaction good agreement available kinetic data, both wild-type mutant versions EF-Tu, indicates ...