3riq

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<StructureSection load='3riq' size='340' side='right'caption='[[3riq]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
<StructureSection load='3riq' size='340' side='right'caption='[[3riq]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3riq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Enterobacteriophage_9na Enterobacteriophage 9na]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RIQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RIQ FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3riq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Siphovirus_9NA Siphovirus 9NA]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RIQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RIQ FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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=3riq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3riq OCA], [https://pdbe.org/3riq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3riq RCSB], [https://www.ebi.ac.uk/pdbsum/3riq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3riq ProSAT]</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=3riq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3riq OCA], [https://pdbe.org/3riq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3riq RCSB], [https://www.ebi.ac.uk/pdbsum/3riq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3riq ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/G8GV21_9CAUD G8GV21_9CAUD]
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Bacteriophages use specific tail proteins to recognize host cells. It is still not understood to molecular detail how the signal is transmitted over the tail to initiate infection. We have analysed in vitro DNA ejection in long-tailed siphovirus 9NA and short-tailed podovirus P22 upon incubation with Salmonella typhimurium lipopolysaccharide (LPS). We showed for the first time that LPS alone was sufficient to elicit DNA release from a siphovirus in vitro. Crystal structure analysis revealed that both phages use similar tailspike proteins for LPS recognition. Tailspike proteins hydrolyse LPS O antigen to position the phage on the cell surface. Thus we were able to compare in vitro DNA ejection processes from two phages with different morphologies with the same receptor under identical experimental conditions. Siphovirus 9NA ejected its DNA about 30 times faster than podovirus P22. DNA ejection is under control of the conformational opening of the particle and has a similar activation barrier in 9NA and P22. Our data suggest that tail morphology influences the efficiencies of particle opening given an identical initial receptor interaction event.
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Tail morphology controls DNA release in two Salmonella phages with one lipopolysaccharide receptor recognition system.,Andres D, Roske Y, Doering C, Heinemann U, Seckler R, Barbirz S Mol Microbiol. 2012 Mar;83(6):1244-53. doi: 10.1111/j.1365-2958.2012.08006.x., Epub 2012 Feb 27. PMID:22364412<ref>PMID:22364412</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3riq" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
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*[[Tailspike protein|Tailspike protein]]
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*[[Tailspike protein 3D structures|Tailspike protein 3D structures]]
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Enterobacteriophage 9na]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Andres, D]]
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[[Category: Siphovirus 9NA]]
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[[Category: Barbirz, S]]
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[[Category: Andres D]]
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[[Category: Doering, C]]
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[[Category: Barbirz S]]
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[[Category: Heinemann, U]]
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[[Category: Doering C]]
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[[Category: Roske, Y]]
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[[Category: Heinemann U]]
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[[Category: Seckler, R]]
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[[Category: Roske Y]]
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[[Category: Endorhamnosidase]]
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[[Category: Seckler R]]
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[[Category: Lipopolysaccharide]]
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[[Category: Right handed beta-helix]]
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[[Category: Tailspike]]
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[[Category: Viral protein]]
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Current revision

Siphovirus 9NA tailspike receptor binding domain

PDB ID 3riq

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Proteopedia Page Contributors and Editors (what is this?)

OCA

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