2J85

B116 of Sulfolobus turreted icosahedral virus (STIV)

「2BLK」から置き換えられました

2J85 の概要

• エントリーDOI: 10.2210/pdb2j85/pdb
• 分子名称: STIV B116 (2 entities in total)
• 機能のキーワード: viral protein, archaeal virus, crenarchaeal virus, b116, stiv, archaea, sulfolobus, crenarchaea, sulfolobus turreted icosahedral virus, hypothetical protein
• 由来する生物種: SULFOLOBUS TURRETED ICOSAHEDRAL VIRUS (STIV)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 28819.49

構造登録者

Larson, E.T.,Reiter, D.,Young, M.J.,Lawrence, C.M. (登録日: 2006-10-19, 公開日: 2006-11-02, 最終更新日: 2024-11-13)

主引用文献

Larson, E.T.,Eilers, B.J.,Reiter, D.,Ortmann, A.C.,Young, M.J.,Lawrence, C.M.
A New DNA Binding Protein Highly Conserved in Diverse Crenarchaeal Viruses
Virology, 363:387-, 2007

PubMed Abstract: Sulfolobus turreted icosahedral virus (STIV) infects Sulfolobus species found in the hot springs of Yellowstone National Park. Its 37 open reading frames (ORFs) generally lack sequence similarity to other genes. One exception, however, is ORF B116. While its function is unknown, orthologs are found in three additional crenarchaeal viral families. Due to the central importance of this protein family to crenarchaeal viruses, we have undertaken structural and biochemical studies of B116. The structure reveals a previously unobserved fold consisting of a five-stranded beta-sheet flanked on one side by three alpha helices. Two subunits come together to form a homodimer with a 10-stranded mixed beta-sheet, where the topology of the central strands resembles an unclosed beta-barrel. Highly conserved loops rise above the surface of the saddle-shaped protein and suggest an interaction with the major groove of DNA. The predicted B116-DNA interaction is confirmed by electrophoretic mobility shift assays.

PubMed: 17336360
DOI: 10.1016/J.VIROL.2007.01.027

実験手法

X-RAY DIFFRACTION (2.39 Å)