2CO5

F93 FROM STIV, a winged-helix DNA-binding protein

2CO5 の概要

• エントリーDOI: 10.2210/pdb2co5/pdb
• 分子名称: VIRAL PROTEIN F93 (2 entities in total)
• 機能のキーワード: viral protein-winged helix complex, winged helix, dna-binding, hth, whth, f93, disulfide bond, stiv, sulfolobus turreted icosahedral virus, viral protein, virus, archaea, crenarchaea, archaeal virus, crenarchaeal virus, thermophilic protein, thermophilic virus, sulfolobus, yellowstone, viral protein/winged helix
• 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: 24000.37

構造登録者

Larson, E.T.,Reiter, D.,Lawrence, C.M. (登録日: 2006-05-25, 公開日: 2006-05-31, 最終更新日: 2024-10-23)

主引用文献

Larson, E.T.,Eilers, B.,Menon, S.,Reiter, D.,Ortmann, A.,Young, M.J.,Lawrence, C.M.
A Winged-Helix Protein from Sulfolobus Turreted Icosahedral Virus Points Toward Stabilizing Disulfide Bonds in the Intracellular Proteins of a Hyperthermophilic Virus.
Virology, 368:249-, 2007

PubMed Abstract: Sulfolobus turreted icosahedral virus (STIV) was the first non-tailed icosahedral virus to be isolated from an archaeal host. Like other archaeal viruses, its 37 open reading frames generally lack sequence similarity to genes with known function. The roles of the gene products in this and other archaeal viruses are thus largely unknown. However, a protein's three-dimensional structure may provide functional and evolutionary insight in cases of minimal sequence similarity. In this vein, the structure of STIV F93 reveals a homodimer with strong similarity to the winged-helix family of DNA-binding proteins. Importantly, an interchain disulfide bond is found at the dimer interface, prompting analysis of the cysteine distribution in the putative intracellular proteins of the viral proteome. The analysis suggests that intracellular disulfide bonds are common in cellular STIV proteins, where they enhance the thermostability of the viral proteome.

PubMed: 17669459
DOI: 10.1016/J.VIROL.2007.06.040

実験手法

X-RAY DIFFRACTION (2.2 Å)