Analysis of RNA Methylation by Phylogenetically Diverse CFR Radical SAdenosylmethionine Enzymes Reveals an Iron-Binding Accessory Domain in a Clostridial Enzyme

doi 10.1021/acs.biochem.9b00197.s001

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Analysis of RNA Methylation by Phylogenetically Diverse CFR Radical SAdenosylmethionine Enzymes Reveals an Iron-Binding Accessory Domain in a Clostridial Enzyme

Full Text

Abstract

Date

Authors

Publisher

Related search

RlmN and CFR Are Radical SAM Enzymes Involved in Methylation of Ribosomal RNA

Structure and Dynamics of the Iron Responsive Element RNA: Implications for Binding of the RNA by Iron Regulatory Binding Proteins

A Conserved Double-Stranded RNA-binding Domain.

Group II Intron Splicing Factors Derived by Diversification of an Ancient RNA-binding Domain

The Crystal Structure of Ribosomal Protein S4 Reveals a Two-Domain Molecule With an Extensive RNA-binding Surface: One Domain Shows Structural Homology to the ETS DNA-binding Motif

Structure of a Hepatitis C Virus RNA Domain in Complex With a Translation Inhibitor Reveals a Binding Mode Reminiscent of Riboswitches

Thermodynamics of Ligand Binding by the Yeast mRNA-capping Enzyme Reveals Different Modes of Binding

Localization of an RNA Binding Element of the Iron Responsive Element Binding Protein Within a Proteolytic Fragment Containing Iron Coordination Ligands

RNA Binding in an Sm Core Domain: X-Ray Structure and Functional Analysis of an Archaeal Sm Protein Complex