1y0q
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(New page: 200px<br /><applet load="1y0q" size="450" color="white" frame="true" align="right" spinBox="true" caption="1y0q, resolution 3.60Å" /> '''Crystal structure of...)
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Revision as of 01:10, 25 November 2007
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Crystal structure of an active group I ribozyme-product complex
Overview
Group I introns are catalytic RNAs capable of orchestrating two sequential, phosphotransesterification reactions that result in self-splicing. To, understand how the group I intron active site facilitates catalysis, we, have solved the structure of an active ribozyme derived from the orf142-I2, intron from phage Twort bound to a four-nucleotide product RNA at a, resolution of 3.6 A. In addition to the three conserved domains, characteristic of all group I introns, the Twort ribozyme has peripheral, insertions characteristic of phage introns. These elements form a ring, that completely envelops the active site, where a snug pocket for, guanosine is formed by a series of stacked base triples. The structure of, the active site reveals three potential binding sites for catalytic, metals, and invokes a role for the 2' hydroxyl of the guanosine substrate, in organization of the active site for catalysis.
About this Structure
1Y0Q is a Protein complex structure of sequences from Staphylococcus phage twort with SPK, MG and SO4 as ligands. Full crystallographic information is available from OCA.
Reference
Crystal structure of a phage Twort group I ribozyme-product complex., Golden BL, Kim H, Chase E, Nat Struct Mol Biol. 2005 Jan;12(1):82-9. Epub 2004 Dec 5. PMID:15580277
Page seeded by OCA on Sun Nov 25 03:17:38 2007
Categories: Protein complex | Staphylococcus phage twort | Chase, E. | Golden, B.L. | Kim, H. | MG | SO4 | SPK | Guanosine-binding | Ribozyme | Rna-folding | Rna-splicing