title: The structural and functional uniqueness of the glmS ribozyme.
abstract: The glmS bacterial ribozyme/riboswitch is found in a number of Gram-positive bacteria, many of which are human pathogens. Investigation of the structure and function of the glmS catalyst will aid in the development of artificial agonists/antagonists that might function as novel antibiotics. The glmS ribozyme is mechanistically unique in that it is the first RNA catalyst identified to require a coenzyme, glucosamine-6-phosphate, for RNA self-cleavage. In addition, it is the first riboswitch identified to utilize self-cleavage as a mode of genetic regulation in metabolism. Significant biochemical and biophysical data exist for the glmS ribozyme and aid in mechanistically understanding the importance of RNA and coenzyme structure to function in acid-base catalysis.
authors.affiliation: Department of Chemistry, Creighton University, Omaha, Nebraska, USA.
authors.forename: Juliane K
authors.initials: JK
authors.lastname: Soukup
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism*; D011487:Protein Conformation; D016337:RNA, Catalytic / Q000737:chemistry / Q000378:metabolism*; D013329:Structure-Activity Relationship; D005945:Glutamine-Fructose-6-Phosphate Transaminase (Isomerizing)
chemical_list: D001426:Bacterial Proteins; D016337:RNA, Catalytic; C000731191:component S, glutamate mutase protein, Bacteria; D005945:Glutamine-Fructose-6-Phosphate Transaminase (Isomerizing)
keywords: Acid–base catalysis; Coenzyme; Riboswitch; Ribozyme; Self-cleavage