1i5l
From Proteopedia
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CRYSTAL STRUCTURE OF AN SM-LIKE PROTEIN (AF-SM1) FROM ARCHAEOGLOBUS FULGIDUS COMPLEXED WITH SHORT POLY-U RNA
Overview
Eukaryotic Sm and Sm-like proteins associate with RNA to form the core, domain of ribonucleoprotein particles involved in pre-mRNA splicing and, other processes. Recently, putative Sm proteins of unknown function have, been identified in ARCHAEA: We show by immunoprecipitation experiments, that the two Sm proteins present in Archaeoglobus fulgidus (AF-Sm1 and, AF-Sm2) associate with RNase P RNA in vivo, suggesting a role in tRNA, processing. The AF-Sm1 protein also interacts specifically with, oligouridylate in vitro. We have solved the crystal structures of this, protein and a complex with RNA. AF-Sm1 forms a seven-membered ring, with, the RNA interacting inside the central cavity on one face of the, doughnut-shaped complex. The bases are bound via stacking and specific, hydrogen bonding contacts in pockets lined by residues highly conserved in, archaeal and eukaryotic Sm proteins, while the phosphates remain solvent, accessible. A comparison with the structures of human Sm protein dimers, reveals closely related monomer folds and intersubunit contacts, indicating that the architecture of the Sm core domain and RNA binding, have been conserved during evolution.
About this Structure
1I5L is a Single protein structure of sequence from Archaeoglobus fulgidus with URI as ligand. Full crystallographic information is available from OCA.
Reference
RNA binding in an Sm core domain: X-ray structure and functional analysis of an archaeal Sm protein complex., Toro I, Thore S, Mayer C, Basquin J, Seraphin B, Suck D, EMBO J. 2001 May 1;20(9):2293-303. PMID:11331594
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