2bbd: Difference between revisions

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Crystal Structure of the STIV MCP

OverviewOverview

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.

About this StructureAbout this Structure

2BBD is a Single protein structure of sequence from Sulfolobus turreted icosahedral virus with as ligand. Full crystallographic information is available from OCA.

ReferenceReference

Structure of an archaeal virus capsid protein reveals a common ancestry to eukaryotic and bacterial viruses., Khayat R, Tang L, Larson ET, Lawrence CM, Young M, Johnson JE, Proc Natl Acad Sci U S A. 2005 Dec 27;102(52):18944-9. Epub 2005 Dec 15. PMID:16357204

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 ==Overview==
-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.
+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.
 ==About this Structure==
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 [[Category: virus]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jan 29 18:20:47 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:35:58 2008''