2vqc

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==Overview==
==Overview==
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Sulfolobus spindle-shaped viruses (SSVs), or Fuselloviridae, are ubiquitous crenarchaeal viruses found in high-temperature acidic hot springs around the world (pH &lt;/=4.0; temperature of &gt;/=70 degrees C). Because they are relatively easy to isolate, they represent the best studied of the crenarchaeal viruses. This is particularly true for the type virus, SSV1, which contains a double-stranded DNA genome of 15.5 kilobases, encoding 34 putative open reading frames. Interestingly, the genome shows little sequence similarity to organisms other than its SSV homologues. Together, sequence similarity and biochemical analyses have suggested functions for only 6 of the 34 open reading frames. Thus, even though SSV1 is the best-studied crenarchaeal virus, functions for most (28) of its open reading frames remain unknown. We have undertaken biochemical and structural studies for the gene product of open reading frame F-93. We find that F-93 exists as a homodimer in solution and that a tight dimer is also present in the 2.7-A crystal structure. Further, the crystal structure reveals a fold that is homologous to the SlyA and MarR subfamilies of winged-helix DNA binding proteins. This strongly suggests that F-93 functions as a transcription factor that recognizes a (pseudo-)palindromic DNA target sequence.
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Fuselloviridae are ubiquitous crenarchaeal viruses found in high-temperature acidic hot springs worldwide. The type virus, Sulfolobus spindle-shaped virus 1 (SSV1), has a double-stranded DNA genome that contains 34 open reading frames (ORFs). Fuselloviral genomes show little similarity to other organisms, generally precluding functional predictions. However, tertiary protein structure can provide insight into protein function. We have thus undertaken a systematic investigation of the SSV1 proteome and report here on the F112 gene product. Biochemical, proteomic and structural studies reveal a monomeric intracellular protein that adopts a winged helix DNA binding fold. Notably, the structure contains an intrachain disulfide bond, prompting analysis of cysteine usage in this and other hyperthermophilic viral genomes. The analysis supports a general abundance of disulfide bonds in the intracellular proteins of hyperthermophilic viruses, and reveals decreased cysteine content in the membrane proteins of hyperthermophilic viruses infecting Sulfolobales. The evolutionary implications of the SSV1 distribution are discussed.
==About this Structure==
==About this Structure==
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==Reference==
==Reference==
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Crystal structure of F-93 from Sulfolobus spindle-shaped virus 1, a winged-helix DNA binding protein., Kraft P, Oeckinghaus A, Kummel D, Gauss GH, Gilmore J, Wiedenheft B, Young M, Lawrence CM, J Virol. 2004 Nov;78(21):11544-50. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15479795 15479795]
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Cysteine usage in Sulfolobus spindle-shaped virus 1 and extension to hyperthermophilic viruses in general., Menon SK, Maaty WS, Corn GJ, Kwok SC, Eilers BJ, Kraft P, Gillitzer E, Young MJ, Bothner B, Lawrence CM, Virology. 2008 Jul 5;376(2):270-8. Epub 2008 May 8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18471851 18471851]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Sulfolobus virus 1]]
[[Category: Sulfolobus virus 1]]
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[[Category: Kraft, P.]]
[[Category: Kraft, P.]]
[[Category: Lawrence, C M.]]
[[Category: Lawrence, C M.]]
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[[Category: Menon, S.]]
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[[Category: Menon, S K.]]
[[Category: Wiedenheft, B.]]
[[Category: Wiedenheft, B.]]
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[[Category: Young, M.]]
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[[Category: Young, M J.]]
[[Category: Crenarchaeal]]
[[Category: Crenarchaeal]]
[[Category: Dna-binding protein]]
[[Category: Dna-binding protein]]
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[[Category: Thermophilic protein]]
[[Category: Thermophilic protein]]
[[Category: Winged-helix]]
[[Category: Winged-helix]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed May 7 08:46:50 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jun 18 12:18:46 2008''

Revision as of 09:18, 18 June 2008

Template:STRUCTURE 2vqc

STRUCTURE OF A DNA BINDING WINGED-HELIX PROTEIN, F-112, FROM SULFOLOBUS SPINDLE-SHAPED VIRUS 1.


Overview

Fuselloviridae are ubiquitous crenarchaeal viruses found in high-temperature acidic hot springs worldwide. The type virus, Sulfolobus spindle-shaped virus 1 (SSV1), has a double-stranded DNA genome that contains 34 open reading frames (ORFs). Fuselloviral genomes show little similarity to other organisms, generally precluding functional predictions. However, tertiary protein structure can provide insight into protein function. We have thus undertaken a systematic investigation of the SSV1 proteome and report here on the F112 gene product. Biochemical, proteomic and structural studies reveal a monomeric intracellular protein that adopts a winged helix DNA binding fold. Notably, the structure contains an intrachain disulfide bond, prompting analysis of cysteine usage in this and other hyperthermophilic viral genomes. The analysis supports a general abundance of disulfide bonds in the intracellular proteins of hyperthermophilic viruses, and reveals decreased cysteine content in the membrane proteins of hyperthermophilic viruses infecting Sulfolobales. The evolutionary implications of the SSV1 distribution are discussed.

About this Structure

2VQC is a Single protein structure of sequence from Sulfolobus virus 1. This structure supersedes the now removed PDB entry 2cmx. Full crystallographic information is available from OCA.

Reference

Cysteine usage in Sulfolobus spindle-shaped virus 1 and extension to hyperthermophilic viruses in general., Menon SK, Maaty WS, Corn GJ, Kwok SC, Eilers BJ, Kraft P, Gillitzer E, Young MJ, Bothner B, Lawrence CM, Virology. 2008 Jul 5;376(2):270-8. Epub 2008 May 8. PMID:18471851 Page seeded by OCA on Wed Jun 18 12:18:46 2008

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