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| | ==The crystal structure of T4 UvsW== | | ==The crystal structure of T4 UvsW== |
| - | <StructureSection load='2oca' size='340' side='right' caption='[[2oca]], [[Resolution|resolution]] 2.70Å' scene=''> | + | <StructureSection load='2oca' size='340' side='right'caption='[[2oca]], [[Resolution|resolution]] 2.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2oca]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bpt4 Bpt4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OCA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2OCA FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2oca]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_virus_T4 Escherichia virus T4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OCA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2OCA FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">uvsW, dar ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10665 BPT4])</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/ATP_diphosphatase ATP diphosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.8 3.6.1.8] </span></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=2oca FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2oca OCA], [https://pdbe.org/2oca PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2oca RCSB], [https://www.ebi.ac.uk/pdbsum/2oca PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2oca ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2oca FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2oca OCA], [http://pdbe.org/2oca PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2oca RCSB], [http://www.ebi.ac.uk/pdbsum/2oca PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2oca ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/UVSW_BPT4 UVSW_BPT4]] DNA helicase that catalyzes branch migration and dissociation of RNA-DNA hybrids. Plays a critical role in a specific recombination pathway involving simple reciprocal exchange. UvsW protein is normally the key regulatory factor in the switch from early to late phage DNA replication. | + | [https://www.uniprot.org/uniprot/UVSW_BPT4 UVSW_BPT4] DNA helicase that catalyzes branch migration and dissociation of RNA-DNA hybrids. Plays a critical role in a specific recombination pathway involving simple reciprocal exchange. UvsW protein is normally the key regulatory factor in the switch from early to late phage DNA replication. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| | Check<jmol> | | Check<jmol> |
| | <jmolCheckbox> | | <jmolCheckbox> |
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/oc/2oca_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/oc/2oca_consurf.spt"</scriptWhenChecked> |
| | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
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| | </div> | | </div> |
| | <div class="pdbe-citations 2oca" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 2oca" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Helicase 3D structures|Helicase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: ATP diphosphatase]] | + | [[Category: Escherichia virus T4]] |
| - | [[Category: Bpt4]] | + | [[Category: Large Structures]] |
| - | [[Category: Kerr, I D]] | + | [[Category: Kerr ID]] |
| - | [[Category: White, S W]] | + | [[Category: White SW]] |
| - | [[Category: Atp-dependant helicase]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Recombination]]
| + | |
| - | [[Category: T4-bacteriophage]]
| + | |
| Structural highlights
Function
UVSW_BPT4 DNA helicase that catalyzes branch migration and dissociation of RNA-DNA hybrids. Plays a critical role in a specific recombination pathway involving simple reciprocal exchange. UvsW protein is normally the key regulatory factor in the switch from early to late phage DNA replication.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The uvsWXY system is implicated in the replication and repair of the bacteriophage T4 genome. Whereas the roles of the recombinase (UvsX) and the recombination mediator protein (UvsY) are known, the precise role of UvsW is unclear. Sequence analysis identifies UvsW as a member of the monomeric SF2 helicase superfamily that translocates nucleic acid substrates via the action of two RecA-like motor domains. Functional homologies to Escherichia coli RecG and biochemical analyses have shown that UvsW interacts with branched nucleic acid substrates, suggesting roles in recombination and the rescue of stalled replication forks. A sequencing error at the 3'-end of the uvsW gene has revealed a second, short open reading frame that encodes a protein of unknown function called UvsW.1. We have determined the crystal structure of UvsW to 2.7A and the NMR solution structure of UvsW.1. UvsW has a four-domain architecture with structural homology to the eukaryotic SF2 helicase, Rad54. A model of the UvsW-ssDNA complex identifies structural elements and conserved residues that may interact with nucleic acid substrates. The NMR solution structure of UvsW.1 reveals a dynamic four-helix bundle with homology to the structure-specific nucleic acid binding module of RecQ helicases.
Crystallographic and NMR analyses of UvsW and UvsW.1 from bacteriophage T4.,Kerr ID, Sivakolundu S, Li Z, Buchsbaum JC, Knox LA, Kriwacki R, White SW J Biol Chem. 2007 Nov 23;282(47):34392-400. Epub 2007 Sep 17. PMID:17878153[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Kerr ID, Sivakolundu S, Li Z, Buchsbaum JC, Knox LA, Kriwacki R, White SW. Crystallographic and NMR analyses of UvsW and UvsW.1 from bacteriophage T4. J Biol Chem. 2007 Nov 23;282(47):34392-400. Epub 2007 Sep 17. PMID:17878153 doi:10.1074/jbc.M705900200
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