Crystal structure of a self-splicing group I intron with both exons Export

@article{adams04, abstract = {The discovery of the RNA self-splicing group I intron provided the first demonstration that not all enzymes are proteins. Here we report the X-ray crystal structure (3.1-\r{A} resolution) of a complete group I bacterial intron in complex with both the 5'- and the 3'-exons. This complex corresponds to the splicing intermediate before the exon ligation step. It reveals how the intron uses structurally unprecedented RNA motifs to select the 5'- and 3'-splice sites. The 5'-exon's 3'-OH is positioned for inline nucleophilic attack on the conformationally constrained scissile phosphate at the intron–3'-exon junction. Six phosphates from three disparate RNA strands converge to coordinate two metal ions that are asymmetrically positioned on opposing sides of the reactive phosphate. This structure represents the first splicing complex to include a complete intron, both exons and an organized active site occupied with metal ions.}, address = {Department of Molecular Biophysics and Biochemistry, 260 Whitney Avenue, Yale University, New Haven, Connecticut 06520-8114, USA.}, author = {Adams, P. L. and Stahley, M. R. and Kosek, A. B. and Wang, J. and Strobel, S. A.}, citeulike-article-id = {669481}, citeulike-linkout-0 = {http://dx.doi.org/10.1038/nature02642}, citeulike-linkout-1 = {http://dx.doi.org/10.1038/nature02642}, citeulike-linkout-2 = {http://view.ncbi.nlm.nih.gov/pubmed/15175762}, citeulike-linkout-3 = {http://www.hubmed.org/display.cgi?uids=15175762}, day = {02}, doi = {10.1038/nature02642}, issn = {0028-0836}, journal = {Nature}, keywords = {azoarcus, crystal, groupi, ribozyme, structure}, month = {June}, number = {6995}, pages = {45--50}, posted-at = {2008-01-12 20:16:35}, priority = {0}, publisher = {Nature Publishing Group}, title = {Crystal structure of a self-splicing group I intron with both exons}, url = {http://dx.doi.org/10.1038/nature02642}, volume = {430}, year = {2004} }

TY - JOUR ID - adams04 L3 - citeulike-article-id:669481 N2 - The discovery of the RNA self-splicing group I intron provided the first demonstration that not all enzymes are proteins. Here we report the X-ray crystal structure (3.1-Å resolution) of a complete group I bacterial intron in complex with both the 5'- and the 3'-exons. This complex corresponds to the splicing intermediate before the exon ligation step. It reveals how the intron uses structurally unprecedented RNA motifs to select the 5'- and 3'-splice sites. The 5'-exon's 3'-OH is positioned for inline nucleophilic attack on the conformationally constrained scissile phosphate at the intron–3'-exon junction. Six phosphates from three disparate RNA strands converge to coordinate two metal ions that are asymmetrically positioned on opposing sides of the reactive phosphate. This structure represents the first splicing complex to include a complete intron, both exons and an organized active site occupied with metal ions. IS - 6995 JF - Nature SN - 0028-0836 AD - Department of Molecular Biophysics and Biochemistry, 260 Whitney Avenue, Yale University, New Haven, Connecticut 06520-8114, USA. EP - 50 TI - Crystal structure of a self-splicing group I intron with both exons PB - Nature Publishing Group VL - 430 SP - 45 KW - azoarcus KW - crystal KW - groupi KW - ribozyme KW - structure AU - Adams, PL AU - Stahley, MR AU - Kosek, AB AU - Wang, J AU - Strobel, SA PY - 2004/06/02/ UR - http://dx.doi.org/10.1038/nature02642 ER -