4ATS

Structure of the ORF273 protein from the Acidianus two-tailed virus

4ATS の概要

• エントリーDOI: 10.2210/pdb4ats/pdb
• 関連するPDBエントリー: 4ART
• 分子名称: STRUCTURAL PROTEIN ORF273 (1 entity in total)
• 機能のキーワード: viral protein, archaeal virus, extremophiles, bicaudavirus, hyper-thermostability
• 由来する生物種: ACIDIANUS TWO-TAILED VIRUS
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 34365.51

構造登録者

Felisberto-Rodrigues, C.,Ortiz-Lombardia, M. (登録日: 2012-05-09, 公開日: 2012-10-24, 最終更新日: 2024-11-20)

主引用文献

Felisberto-Rodrigues, C.,Blangy, S.,Goulet, A.,Vestergaard, G.,Cambillau, C.,Garrett, R.A.,Ortiz-Lombardia, M.
Crystal Structure of Atv(Orf273), a New Fold for a Thermo-and Acido-Stable Protein from the Acidianus Two-Tailed Virus.
Plos One, 7:45847-, 2012

PubMed Abstract: Acidianus two-tailed virus (ATV) infects crenarchaea of the genus Acidianus living in terrestrial thermal springs at extremely high temperatures and low pH. ATV is a member of the Bicaudaviridae virus family and undergoes extra-cellular development of two tails, a process that is unique in the viral world. To understand this intriguing phenomenon, we have undertaken structural studies of ATV virion proteins and here we present the crystal structure of one of these proteins, ATV(ORF273). ATV(ORF273) forms tetramers in solution and a molecular envelope is provided for the tetramer, computed from small-angle X-ray scattering (SAXS) data. The crystal structure has properties typical of hyperthermostable proteins, including a relatively high number of salt bridges. However, the protein also exhibits flexible loops and surface pockets. Remarkably, ATV(ORF273) displays a new α + β protein fold, consistent with the absence of homologues of this protein in public sequence databases.

PubMed: 23056221
DOI: 10.1371/JOURNAL.PONE.0045847

実験手法

X-RAY DIFFRACTION (3.85 Å)