1M5Q
Crystal structure of a novel Sm-like archaeal protein from Pyrobaculum aerophilum
1M5Q の概要
エントリーDOI | 10.2210/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: 12668760DOI: 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) |
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