2BBD

Crystal Structure of the STIV MCP

2BBD の概要

• エントリーDOI: 10.2210/pdb2bbd/pdb
• 分子名称: coat protein, (4S)-2-METHYL-2,4-PENTANEDIOL (3 entities in total)
• 機能のキーワード: archaea, hyperthermophile, virus, evolution, crystal, viral protein
• 由来する生物種: Sulfolobus turreted icosahedral virus
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 156985.19

構造登録者

Khayat, R. (登録日: 2005-10-17, 公開日: 2005-12-06, 最終更新日: 2024-10-30)

主引用文献

Khayat, R.,Tang, L.,Larson, E.T.,Lawrence, C.M.,Young, M.,Johnson, J.E.
Structure of an archaeal virus capsid protein reveals a common ancestry to eukaryotic and bacterial viruses.
Proc.Natl.Acad.Sci.Usa, 102:18944-18949, 2005

PubMed Abstract: Archaea and their viruses are poorly understood when compared with the Eukarya and Bacteria domains of life. We report here the crystal structure of the major capsid protein (MCP) of the Sulfolobus turreted icosahedral virus, an archaeal virus isolated from an acidic hot spring (pH 2-4, 72-92 degrees C) in Yellowstone National Park. The structure is nearly identical to the MCP structures of the eukaryotic Paramecium bursaria Chlorella virus, and the bacteriophage PRD1, and shows a common fold with the mammalian adenovirus. Structural analysis of the capsid architecture, determined by fitting the subunit into the electron cryomicroscopy reconstruction of the virus, identified a number of key interactions that are akin to those observed in adenovirus and PRD1. The similar capsid proteins and capsid architectures strongly suggest that these viral capsids originated and evolved from a common ancestor. Hence, this work provides a previously undescribed example of a viral relationship spanning the three domains of life (Eukarya, Bacteria, and Archaea). The MCP structure also provides insights into the stabilizing forces required for extracellular hyperthermophilic proteins to tolerate high-temperature hot springs.

PubMed: 16357204
DOI: 10.1073/pnas.0506383102

実験手法

X-RAY DIFFRACTION (2.04 Å)