Structure and assembly of an augmented Sm-like archaeal protein 14-mer.

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.

authors

Mura C,Phillips M,Kozhukhovsky A,Eisenberg D

doi

10.1073/pnas.0538042100

keywords:

subject

Has Abstract

pub_date

2003-04-15 00:00:00

pages

4539-44

issue

8

eissn

0027-8424

issn

1091-6490

pii

0538042100

journal_volume

100

pub_type

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