Metal ion coordination to 2′ functionality of guanosine mediates substrate-guanosine coupling in group I ribozymes: Implications for conserved role of metal ions and for variability in RNA folding in ribozyme catalysis

Inorganica Chimica Acta

Volumn 357, Issue 13, 2004, Pages 3934-3942

  Kuo, Louis ^a   Perera, Nicholas ^a   Tarpo, Shyla ^a  

^a LEWIS AND CLARK COLLEGE   (United States)

Author keywords

Azoarcus ribozyme; Guanosine; Substrate; Tetrahymena ribozyme

Indexed keywords

BIOCHEMISTRY; BIOMOLECULES; CATALYSIS; CONFORMATIONS; COOPERATIVE COMMUNICATION; METAL IONS; SUBSTRATES;

CONFORMATIONAL CHANGE; COOPERATIVE BINDING; GUANOSINES; METAL INTERACTIONS; METAL-ION COORDINATION; PHOSPHORYL TRANSFER; RIBOZYMES; SUBSTRATE COUPLINGS;

METALS;

GUANOSINE; METAL ION; RIBOZYME; RNA;

ARTICLE; AZOARCUS; CATALYSIS; CHEMICAL INTERACTION; CHEMICAL STRUCTURE; INTRON; PHYLOGENY; PROTEIN BINDING; RNA SPLICING; TEMPERATURE DEPENDENCE; TETRAHYMENA;

EID: 14344253887     PISSN: 00201693     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ica.2004.06.060     Document Type: Article

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48. Since submission of this manuscript, a crystal structure of the Azoarcus intron in complex with both the 5′ and 3′ exons shows two divalent metal ions positioned in the catalytic site. One metal ion (M2) coordinates to the 2′-OH of the guanosine and hydrogen bonded to the scissile phosphate oxygen atom (pro-Rp); this would be the Mc metal ion designated in this paper. P.L. Adams, M.R. Stahley, A.B. Kosek, J. Wang, and S.A. Strobel Nature 430 2004 45