2mlg: Difference between revisions

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{{STRUCTURE_2mlg|  PDB=2mlg | SCENE= }}
==Stf76 from the Sulfolobus islandicus plasmid-virus pSSVx==
===Stf76 from the Sulfolobus islandicus plasmid-virus pSSVx===
<StructureSection load='2mlg' size='340' side='right' caption='[[2mlg]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2mlg]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Fuselloviridae Fuselloviridae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MLG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2MLG FirstGlance]. <br>
</td></tr><tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2mlg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mlg OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2mlg RCSB], [http://www.ebi.ac.uk/pdbsum/2mlg PDBsum]</span></td></tr>
<table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The hybrid plasmid-virus pSSVx from Sulfolobus islandicus presents an open reading frame encoding a 76 amino acid protein, namely Stf76, that does not show significant sequence homology with any protein with known 3D structure. The recombinant protein recognizes specifically two DNA-binding sites located in its own promoter, thus suggesting an auto-regulated role of its expression. Circular dichroism, spectrofluorimetric, light scattering and isothermal titration calorimetry experiments indicated a 2:1 molar ratio (protein:DNA) upon binding to the DNA target containing a single site. Furthermore, the solution structure of Stf76, determined by nuclear magnetic resonance (NMR) using chemical shift Rosetta software, has shown that the protein assumes a winged helix-turn-helix fold. NMR chemical shift perturbation analysis has been performed for the identification of the residues responsible for DNA interaction. In addition, a model of the Stf76-DNA complex has been built using as template a structurally related homolog.


==About this Structure==
Structural and functional studies of Stf76 from the Sulfolobus islandicus plasmid-virus pSSVx: a novel peculiar member of the winged helix-turn-helix transcription factor family.,Contursi P, Farina B, Pirone L, Fusco S, Russo L, Bartolucci S, Fattorusso R, Pedone E Nucleic Acids Res. 2014 May 1;42(9):5993-6011. doi: 10.1093/nar/gku215. Epub 2014, Mar 25. PMID:24682827<ref>PMID:24682827</ref>
[[2mlg]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MLG OCA].
 
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
</div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Fuselloviridae]]
[[Category: Farina, B.]]
[[Category: Farina, B.]]
[[Category: Fattorusso, R.]]
[[Category: Fattorusso, R.]]

Revision as of 07:38, 4 June 2014

Stf76 from the Sulfolobus islandicus plasmid-virus pSSVxStf76 from the Sulfolobus islandicus plasmid-virus pSSVx

Structural highlights

2mlg is a 1 chain structure with sequence from Fuselloviridae. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:FirstGlance, OCA, RCSB, PDBsum

Publication Abstract from PubMed

The hybrid plasmid-virus pSSVx from Sulfolobus islandicus presents an open reading frame encoding a 76 amino acid protein, namely Stf76, that does not show significant sequence homology with any protein with known 3D structure. The recombinant protein recognizes specifically two DNA-binding sites located in its own promoter, thus suggesting an auto-regulated role of its expression. Circular dichroism, spectrofluorimetric, light scattering and isothermal titration calorimetry experiments indicated a 2:1 molar ratio (protein:DNA) upon binding to the DNA target containing a single site. Furthermore, the solution structure of Stf76, determined by nuclear magnetic resonance (NMR) using chemical shift Rosetta software, has shown that the protein assumes a winged helix-turn-helix fold. NMR chemical shift perturbation analysis has been performed for the identification of the residues responsible for DNA interaction. In addition, a model of the Stf76-DNA complex has been built using as template a structurally related homolog.

Structural and functional studies of Stf76 from the Sulfolobus islandicus plasmid-virus pSSVx: a novel peculiar member of the winged helix-turn-helix transcription factor family.,Contursi P, Farina B, Pirone L, Fusco S, Russo L, Bartolucci S, Fattorusso R, Pedone E Nucleic Acids Res. 2014 May 1;42(9):5993-6011. doi: 10.1093/nar/gku215. Epub 2014, Mar 25. PMID:24682827[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Contursi P, Farina B, Pirone L, Fusco S, Russo L, Bartolucci S, Fattorusso R, Pedone E. Structural and functional studies of Stf76 from the Sulfolobus islandicus plasmid-virus pSSVx: a novel peculiar member of the winged helix-turn-helix transcription factor family. Nucleic Acids Res. 2014 May 1;42(9):5993-6011. doi: 10.1093/nar/gku215. Epub 2014, Mar 25. PMID:24682827 doi:http://dx.doi.org/10.1093/nar/gku215
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