2co5

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{{STRUCTURE_2co5| PDB=2co5 | SCENE= }}
{{STRUCTURE_2co5| PDB=2co5 | SCENE= }}
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'''F93 FROM STIV, A WINGED-HELIX DNA-BINDING PROTEIN'''
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===F93 FROM STIV, A WINGED-HELIX DNA-BINDING PROTEIN===
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==Overview==
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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.
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The line below this paragraph, {{ABSTRACT_PUBMED_17669459}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 17669459 is the PubMed ID number.
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{{ABSTRACT_PUBMED_17669459}}
==About this Structure==
==About this Structure==
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==Reference==
==Reference==
A winged-helix protein from Sulfolobus turreted icosahedral virus points toward stabilizing disulfide bonds in the intracellular proteins of a hyperthermophilic virus., Larson ET, Eilers B, Menon S, Reiter D, Ortmann A, Young MJ, Lawrence CM, Virology. 2007 Nov 25;368(2):249-61. Epub 2007 Jul 31. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17669459 17669459]
A winged-helix protein from Sulfolobus turreted icosahedral virus points toward stabilizing disulfide bonds in the intracellular proteins of a hyperthermophilic virus., Larson ET, Eilers B, Menon S, Reiter D, Ortmann A, Young MJ, Lawrence CM, Virology. 2007 Nov 25;368(2):249-61. Epub 2007 Jul 31. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17669459 17669459]
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The structure of a thermophilic archaeal virus shows a double-stranded DNA viral capsid type that spans all domains of life., Rice G, Tang L, Stedman K, Roberto F, Spuhler J, Gillitzer E, Johnson JE, Douglas T, Young M, Proc Natl Acad Sci U S A. 2004 May 18;101(20):7716-20. Epub 2004 May 3. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15123802 15123802]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Sulfolobus turreted icosahedral virus]]
[[Category: Sulfolobus turreted icosahedral virus]]
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[[Category: Whth]]
[[Category: Whth]]
[[Category: Winged helix]]
[[Category: Winged helix]]
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Revision as of 12:35, 27 July 2008

Template:STRUCTURE 2co5

F93 FROM STIV, A WINGED-HELIX DNA-BINDING PROTEIN

Template:ABSTRACT PUBMED 17669459

About this Structure

2CO5 is a Single protein structure of sequence from Sulfolobus turreted icosahedral virus. Full crystallographic information is available from OCA.

Reference

A winged-helix protein from Sulfolobus turreted icosahedral virus points toward stabilizing disulfide bonds in the intracellular proteins of a hyperthermophilic virus., Larson ET, Eilers B, Menon S, Reiter D, Ortmann A, Young MJ, Lawrence CM, Virology. 2007 Nov 25;368(2):249-61. Epub 2007 Jul 31. PMID:17669459

The structure of a thermophilic archaeal virus shows a double-stranded DNA viral capsid type that spans all domains of life., Rice G, Tang L, Stedman K, Roberto F, Spuhler J, Gillitzer E, Johnson JE, Douglas T, Young M, Proc Natl Acad Sci U S A. 2004 May 18;101(20):7716-20. Epub 2004 May 3. PMID:15123802

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