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1M5Q

Crystal structure of a novel Sm-like archaeal protein from Pyrobaculum aerophilum

1M5Q の概要
エントリーDOI10.2210/pdb1m5q/pdb
関連するPDBエントリー1D3B 1I4K 1I8F 1JBM
分子名称small nuclear ribonucleoprotein homolog, CADMIUM ION, SODIUM ION, ... (6 entities in total)
機能のキーワードob-like fold, b-sheet toroid, 14-mer, cadmium-binding site, translation
由来する生物種Pyrobaculum aerophilum
タンパク質・核酸の鎖数28
化学式量合計425487.61
構造登録者
Mura, C.,Phillips, M.,Kozhukhovsky, A.,Eisenberg, D. (登録日: 2002-07-09, 公開日: 2003-03-18, 最終更新日: 2024-10-30)
主引用文献Mura, C.,Phillips, M.,Kozhukhovsky, A.,Eisenberg, D.
Structure and assembly of an augmented Sm-like archaeal protein 14-mer
Proc.Natl.Acad.Sci.USA, 100:4539-4544, 2003
Cited by
PubMed 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.
PubMed: 12668760
DOI: 10.1073/pnas.0538042100
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2 Å)
構造検証レポート
Validation report summary of 1m5q
検証レポート(詳細版)ダウンロードをダウンロード

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件を2025-04-09に公開中

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