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PMID: 11331747 Published · ppublish English Journal Article Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

The crystal structure of a heptameric archaeal Sm protein: Implications for the eukaryotic snRNP core.

Mura C, Cascio D, Sawaya MR, Eisenberg DS

Abstract

Sm proteins form the core of small nuclear ribonucleoprotein particles (snRNPs), making them key components of several mRNA-processing assemblies, including the spliceosome. We report the 1.75-A crystal structure of SmAP, an Sm-like archaeal protein that forms a heptameric ring perforated by a cationic pore. In addition to providing direct evidence for such an assembly in eukaryotic snRNPs, this structure (i) shows that SmAP homodimers are structurally similar to human Sm heterodimers, (ii) supports a gene duplication model of Sm protein evolution, and (iii) offers a model of SmAP bound to single-stranded RNA (ssRNA) that explains Sm binding-site specificity. The pronounced electrostatic asymmetry of the SmAP surface imparts directionality to putative SmAP-RNA interactions.

MeSH Terms
Amino Acid Sequence Archaea/chemistry Archaeal Proteins/chemistry,metabolism Binding Sites Models, Molecular Molecular Sequence Data Ribonucleoproteins, Small Nuclear/chemistry,metabolism Sequence Homology, Amino Acid
Chemicals
Archaeal Proteins Ribonucleoproteins, Small Nuclear SmAP protein, Pyrobaculum aerophilum
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Mura C
University of California at Los Angeles-Department of Energy Laboratory of Structural Biology and Molecular Medicine, 201 Boyer Hall/Molecular Biology Institute, Box 951570, Los Angeles, CA 90095-1570, USA.
Cascio D
Sawaya M R
Eisenberg D S
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
Published
2001-05-08
Epub
2001-00-01
Pages
5532-7
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC33247
Subset
IM
Databases
PDB
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