2co5

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(New page: 200px<br /><applet load="2co5" size="350" color="white" frame="true" align="right" spinBox="true" caption="2co5, resolution 2.20&Aring;" /> '''F93 FROM STIV, A WIN...)
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==Overview==
==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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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.
==About this Structure==
==About this Structure==
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==Reference==
==Reference==
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=17669459 17669459]
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=17669459 17669459]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Sulfolobus turreted icosahedral virus]]
[[Category: Sulfolobus turreted icosahedral virus]]
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[[Category: Larson, E.T.]]
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[[Category: Larson, E T.]]
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[[Category: Lawrence, C.M.]]
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[[Category: Lawrence, C M.]]
[[Category: Reiter, D.]]
[[Category: Reiter, D.]]
[[Category: archaea]]
[[Category: archaea]]
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[[Category: winged helix]]
[[Category: winged helix]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 12:12:15 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:50:44 2008''

Revision as of 14:50, 21 February 2008

Image:2co5.gif

2co5, resolution 2.20Å

Drag the structure with the mouse to rotate

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

Overview

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.

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

Page seeded by OCA on Thu Feb 21 16:50:44 2008

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