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 alpha/beta C-terminal domain. The structure reveals an unexpected SmAP3 14-mer that is perforated by a cylindrical pore and is bound to 14 cadmium (Cd(2+)) ions. Individual heptamers adopt either "apical" or "equatorial" conformations that chelate Cd(2+) 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.
journal_name
Proc Natl Acad Sci U S Aauthors
Mura C,Phillips M,Kozhukhovsky A,Eisenberg Ddoi
10.1073/pnas.0538042100keywords:
subject
Has Abstractpub_date
2003-04-15 00:00:00pages
4539-44issue
8eissn
0027-8424issn
1091-6490pii
0538042100journal_volume
100pub_type
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更新日期:2020-12-08 00:00:00