Backbone Dynamics ofEscherichia coliRibonuclease HI: Correlations with Structure and Function in an Active Enzyme

摘要: Abstract Ribonuclease H is an endonuclease that hydrolyzes the RNA moiety of RNA–DNA duplex molecules.Escherichia coliribonuclease involved in DNA replication, and retroviral ribonuclease essential for reverse transcription viral genome. To characterize intramolcular dynamical properties ofE. H, spin-lattic relaxation rate constants, spin-spin constants steady state nuclear Overhauser effects the15N spins were measured by using proton-detected heteronuclear NMR spectroscopy. The data analyzed a series models conjunction with statistical model selection protocol. exhibits complex array features, most notably parallel β-strands principal five-stranded β-sheet, coiled-coil helical interface, active site, loop regions surrounding site. are correlated local structural environments suggest possible relationships to functional H. Results forE. compared previously reported results human immunodeficiancy virus type 1 domain transcriptase.