1SKV

Crystal Structure of D-63 from Sulfolobus Spindle Virus 1

1SKV の概要

• エントリーDOI: 10.2210/pdb1skv/pdb
• 分子名称: Hypothetical 7.5 kDa protein (2 entities in total)
• 機能のキーワード: sulfolobus spindle virus, ssv, archaeal, crenarchaeal, helix-turn-helix, four helix bundle, viral protein
• 由来する生物種: Sulfolobus virus 1
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 33609.69

構造登録者

Kraft, P.,Kummel, D.,Oeckinghaus, A.,Gauss, G.H.,Wiedenheft, B.,Young, M.,Lawrence, C.M. (登録日: 2004-03-05, 公開日: 2004-07-13, 最終更新日: 2024-11-13)

主引用文献

Kraft, P.,Oeckinghaus, A.,Gauss, G.H.,Wiedenheft, B.,Young, M.,Lawrence, C.M.
Structure of d-63 from sulfolobus spindle-shaped virus 1: surface properties of the dimeric four-helix bundle suggest an adaptor protein function
J.Virol., 78:7438-7442, 2004

PubMed Abstract: Sulfolobus spindle-shaped virus 1 (SSV1) and its fusellovirus homologues can be found in many acidic (pH or=70 degrees C) around the world. SSV1 contains a 15.5-kb double-stranded DNA genome that encodes 34 proteins with greater than 50 amino acids. A site-specific integrase and a DnaA-like protein have been previously identified by sequence homology, and three structural proteins have been isolated from purified virus and identified by N-terminal sequencing (VP1, VP2, and VP3). The functions of the remaining 29 proteins are currently unknown. To assign functions to these proteins, we have initiated biochemical and structural studies on the SSV1 proteome. Here we report the structure of SSV1 D-63. The structure reveals a helix-turn-helix motif that dimerizes to form an antiparallel four-helix bundle. Mapping residues conserved among three fusellovirus isolates onto the structure shows that one face of the rod-shaped molecule is highly conserved. This conserved surface spans the dimer axis and thus exhibits 2-fold symmetry. Two smaller conserved patches, also related by 2-fold symmetry, are found on the opposite face of the molecule. All of these conserved surfaces are devoid of clefts or pockets typically used to bind small molecules, suggesting that D-63 may function as an adaptor protein in macromolecular assembly.

PubMed: 15220417
DOI: 10.1128/JVI.78.14.7438-7442.2004

実験手法

X-RAY DIFFRACTION (2.6 Å)