Crystal structure of the lysine riboswitch regulatory mRNA element.
Ontology highlight
ABSTRACT: Riboswitches are metabolite-sensitive elements found in mRNAs that control gene expression through a regulatory secondary structural switch. Along with regulation of lysine biosynthetic genes, mutations within the lysine-responsive riboswitch (L-box) play a role in the acquisition of resistance to antimicrobial lysine analogs. To understand the structural basis for lysine binding, we have determined the 2.8 angstroms resolution crystal structure of lysine bound to the Thermotoga maritima asd lysine riboswitch ligand-binding domain. The structure reveals a complex architecture scaffolding a binding pocket completely enveloping lysine. Mutations conferring antimicrobial resistance cluster around this site as well as highly conserved long range interactions, indicating that they disrupt lysin
SUBMITTER: Garst AD
PROVIDER: S-EPMC2504901 | biostudies-literature | 2008 Aug
REPOSITORIES: biostudies-literature
ACCESS DATA