Structure and assembly of an augmented Sm-like archaeal protein 14-mer
- *Howard Hughes Medical Institute, Molecular Biology Institute, and Department of Energy Institute for Genomics and Proteomics, 201 Boyer Hall/ Molecular Biology Institute, University of California, Box 951570, Los Angeles, CA 90095-1570; and† Departments of Chemistry and Biochemistry and Biological Chemistry, University of California, Los Angeles, CA 90095
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Contributed by David Eisenberg
Abstract
To better understand the roles of Sm proteins in forming the cores of many RNA-processing ribonucleoproteins, we determined the crystal structure of an atypical Sm-like archaeal protein (SmAP3) in which the conserved Sm domain is augmented by a previously uncharacterized, mixed α/β C-terminal domain. The structure reveals an unexpected SmAP3 14-mer that is perforated by a cylindrical pore and is bound to 14 cadmium (Cd2+) ions. Individual heptamers adopt either “apical” or “equatorial” conformations that chelate Cd2+ differently. SmAP3 forms supraheptameric oligomers (SmAP3)n = 7,14,28 in solution, and assembly of the asymmetric 14-mer is modulated by differential divalent cation-binding in apical and equatorial subunits. Phylogenetic and sequence analyses substantiate SmAP3s as a unique subset of SmAPs. These results distinguish SmAP3s from other Sm proteins and provide a model for the structure and properties of Sm proteins >100 residues in length, e.g., several human Sm proteins.
Footnotes
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↵ ‡ To whom correspondence should be addressed. E-mail: david{at}mbi.ucla.edu.
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Data deposition: The atomic coordinates and structure factors have been deposited in the Protein Data Bank, www.rcsb.org (PDB ID code ).
- Abbreviations:
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RNP, ribonucleoprotein
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snRNP, small nuclear RNP
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SmAP, Sm-like archaeal protein
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NCS, noncrystallographic symmetry
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a.u., asymmetric unit
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MAD, multiwavelength anomalous dispersion
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rmsd, rms deviation
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Afu, Archaeoglobus fulgidus
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Pae, Pyrobaculum aerophilum
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Mth, Methanobacterium thermautotrophicum
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CTD, C-terminal domain
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ssRNA, single-stranded RNA
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UMP, uridine-5′-monophosphate
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- Copyright © 2003, The National Academy of Sciences





