2vqc
From Proteopedia
(Difference between revisions)
| (9 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | [[Image:2vqc.jpg|left|200px]] | ||
| - | + | ==Structure of a DNA binding winged-helix protein, F-112, from Sulfolobus Spindle-shaped Virus 1.== | |
| - | + | <StructureSection load='2vqc' size='340' side='right'caption='[[2vqc]], [[Resolution|resolution]] 2.30Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[2vqc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Sulfolobus_spindle-shaped_virus_1 Sulfolobus spindle-shaped virus 1]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2cmx 2cmx]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VQC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VQC FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | |
| - | --> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2vqc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vqc OCA], [https://pdbe.org/2vqc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vqc RCSB], [https://www.ebi.ac.uk/pdbsum/2vqc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vqc ProSAT]</span></td></tr> |
| - | + | </table> | |
| - | + | == Function == | |
| - | ''' | + | [https://www.uniprot.org/uniprot/F112_SSV1 F112_SSV1] Essential for virus function.<ref>PMID:10430570</ref> |
| - | + | <div style="background-color:#fffaf0;"> | |
| - | + | == Publication Abstract from PubMed == | |
| - | == | + | |
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. | 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. | ||
| - | + | 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<ref>PMID:18471851</ref> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | [[Category: | + | <div class="pdbe-citations 2vqc" style="background-color:#fffaf0;"></div> |
| - | [[Category: Sulfolobus virus 1]] | + | == References == |
| - | [[Category: Corn | + | <references/> |
| - | [[Category: Kraft | + | __TOC__ |
| - | [[Category: Lawrence | + | </StructureSection> |
| - | [[Category: Menon | + | [[Category: Large Structures]] |
| - | [[Category: Wiedenheft | + | [[Category: Sulfolobus spindle-shaped virus 1]] |
| - | [[Category: Young | + | [[Category: Corn GJ]] |
| - | + | [[Category: Kraft P]] | |
| - | + | [[Category: Lawrence CM]] | |
| - | + | [[Category: Menon SK]] | |
| - | + | [[Category: Wiedenheft B]] | |
| - | + | [[Category: Young MJ]] | |
| - | + | ||
| - | + | ||
Current revision
Structure of a DNA binding winged-helix protein, F-112, from Sulfolobus Spindle-shaped Virus 1.
| |||||||||||
