The change of corrin-amides to carboxylates leads to altered structures of the B12-responding btuB riboswitch.
By applying four different acid derivatives of vitamin B(12), we demonstrate that the H-bonding pattern and the electrostatic environment provided by each side chain of the corrin ring are crucial for the correct structural rearrangement of the btuB riboswitch of E. coli.
Gallo
Sofia
S
Institute of Inorganic Chemistry, University of Zürich, Winterthurerstrasse 190, CH-8057 Zürich, Switzerland.
Mundwiler
Stefan
S
Alberto
Roger
R
Sigel
Roland K O
RK
D000577:Amides / Q000737:chemistry*; D001425:Bacterial Outer Membrane Proteins / Q000737:chemistry* / Q000378:metabolism; D002264:Carboxylic Acids / Q000737:chemistry*; D045728:Corrinoids / Q000737:chemistry*; D004926:Escherichia coli / Q000737:chemistry* / Q000378:metabolism; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000378:metabolism; D006860:Hydrogen Bonding; D026901:Membrane Transport Proteins / Q000737:chemistry* / Q000378:metabolism; D008968:Molecular Conformation; D015394:Molecular Structure; D012313:RNA / Q000737:chemistry / Q000378:metabolism; D055672:Static Electricity; D014805:Vitamin B 12 / Q000737:chemistry* / Q000378:metabolism
D000577:Amides; D001425:Bacterial Outer Membrane Proteins; C044592:BtuB protein, E coli; D002264:Carboxylic Acids; D045728:Corrinoids; D029968:Escherichia coli Proteins; D026901:Membrane Transport Proteins; C473700:corrin; D012313:RNA; D014805:Vitamin B 12