1gid
From Proteopedia
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CRYSTAL STRUCTURE OF A GROUP I RIBOZYME DOMAIN: PRINCIPLES OF RNA PACKING
Overview
Group I self-splicing introns catalyze their own excision from precursor, RNAs by way of a two-step transesterification reaction. The catalytic core, of these ribozymes is formed by two structural domains. The 2.8-angstrom, crystal structure of one of these, the P4-P6 domain of the Tetrahymena, thermophila intron, is described. In the 160-nucleotide domain, a sharp, bend allows stacked helices of the conserved core to pack alongside, helices of an adjacent region. Two specific long-range interactions clamp, the two halves of the domain together: a two-Mg2+-coordinated, adenosine-rich corkscrew plugs into the minor groove of a helix, and a, GAAA hairpin loop binds to a conserved 11-nucleotide internal loop. Metal-, and ribose-mediated backbone contacts further stabilize the close, side-by-side helical packing. The structure indicates the extent of RNA, packing required for the function of large ribozymes, the spliceosome, and, the ribosome.
About this Structure
1GID is a Protein complex structure of sequences from [1] with MG and NCO as ligands. Full crystallographic information is available from OCA.
Reference
Crystal structure of a group I ribozyme domain: principles of RNA packing., Cate JH, Gooding AR, Podell E, Zhou K, Golden BL, Kundrot CE, Cech TR, Doudna JA, Science. 1996 Sep 20;273(5282):1678-85. PMID:8781224
Page seeded by OCA on Sun Nov 25 01:22:26 2007
