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

@article{citeulike:2827121, abstract = {Ribonuclease H is an endonuclease that hydrolyzes the RNA moiety of RNA-DNA duplex molecules.Escherichia coliribonuclease H is involved in DNA replication, and retroviral ribonuclease H is essential for reverse transcription of the viral genome. To characterize the intramolcular dynamical properties ofE. coliribonuclease H, spin-lattic relaxation rate constants, spin-spin relaxation rate constants and steady state nuclear Overhauser effects for the15N nuclear spins were measured by using proton-detected heteronuclear NMR spectroscopy. The relaxation data were analyzed by using a series of dynamical models in conjunction with a statistical model selection protocol. Ribonuclease H exhibits a complex array of dynamical features, most notably in the parallel [beta]-strands of the principal five-stranded [beta]-sheet, the coiled-coil helical interface, the active site, and the loop regions surrounding the active site. The dynamical properties are correlated with local structural environments of the15N spins and suggest possible relationships to the functional properties of ribonuclease H. Results forE. coliribonuclease H are compared to previously reported results for the human immunodeficiancy virus type 1 ribonuclease H domain of reverse transcriptase.}, author = {Mandel, Arthur M. and Akke, Mikael and Palmer, Iii}, citeulike-article-id = {2827121}, citeulike-linkout-0 = {http://dx.doi.org/10.1006/jmbi.1994.0073}, citeulike-linkout-1 = {http://www.sciencedirect.com/science/article/B6WK7-45S98CR-63/1/c8fff66033b9a7b3ade6bb09d6e5a2d4}, day = {10}, doi = {10.1006/jmbi.1994.0073}, journal = {Journal of Molecular Biology}, keywords = {computation, dynamics, model-free, nmr-methods, relaxation}, month = {February}, number = {1}, pages = {144--163}, posted-at = {2008-05-23 23:16:39}, priority = {4}, title = {Backbone Dynamics ofEscherichia coliRibonuclease HI: Correlations with Structure and Function in an Active Enzyme}, url = {http://dx.doi.org/10.1006/jmbi.1994.0073}, volume = {246}, year = {1995} }

TY - JOUR ID - citeulike:2827121 L3 - citeulike-article-id:2827121 N2 - Ribonuclease H is an endonuclease that hydrolyzes the RNA moiety of RNA-DNA duplex molecules.Escherichia coliribonuclease H is involved in DNA replication, and retroviral ribonuclease H is essential for reverse transcription of the viral genome. To characterize the intramolcular dynamical properties ofE. coliribonuclease H, spin-lattic relaxation rate constants, spin-spin relaxation rate constants and steady state nuclear Overhauser effects for the15N nuclear spins were measured by using proton-detected heteronuclear NMR spectroscopy. The relaxation data were analyzed by using a series of dynamical models in conjunction with a statistical model selection protocol. Ribonuclease H exhibits a complex array of dynamical features, most notably in the parallel [beta]-strands of the principal five-stranded [beta]-sheet, the coiled-coil helical interface, the active site, and the loop regions surrounding the active site. The dynamical properties are correlated with local structural environments of the15N spins and suggest possible relationships to the functional properties of ribonuclease H. Results forE. coliribonuclease H are compared to previously reported results for the human immunodeficiancy virus type 1 ribonuclease H domain of reverse transcriptase. IS - 1 JF - Journal of Molecular Biology EP - 163 TI - Backbone Dynamics ofEscherichia coliRibonuclease HI: Correlations with Structure and Function in an Active Enzyme VL - 246 SP - 144 KW - computation KW - dynamics KW - model-free KW - nmr-methods KW - relaxation AU - Mandel, Arthur AU - Akke, Mikael AU - Palmer, Iii PY - 1995/02/10/ UR - http://dx.doi.org/10.1006/jmbi.1994.0073 ER -