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4jpp

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Current revision (12:05, 1 March 2024) (edit) (undo)
 
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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4jpp]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_virus_phiX174 Escherichia virus phiX174]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JPP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4JPP FirstGlance]. <br>
<table><tr><td colspan='2'>[[4jpp]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_virus_phiX174 Escherichia virus phiX174]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JPP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4JPP FirstGlance]. <br>
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</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=4jpp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jpp OCA], [https://pdbe.org/4jpp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4jpp RCSB], [https://www.ebi.ac.uk/pdbsum/4jpp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4jpp ProSAT]</span></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]] 2.4&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4jpp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jpp OCA], [https://pdbe.org/4jpp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4jpp RCSB], [https://www.ebi.ac.uk/pdbsum/4jpp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4jpp ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[https://www.uniprot.org/uniprot/H_BPPHS H_BPPHS] Probably triggers with protein G the injection of the phage DNA into the host upon conformational changes induced by virus-host receptor interaction.<ref>PMID:10739948</ref> <ref>PMID:16143459</ref>
[https://www.uniprot.org/uniprot/H_BPPHS H_BPPHS] Probably triggers with protein G the injection of the phage DNA into the host upon conformational changes induced by virus-host receptor interaction.<ref>PMID:10739948</ref> <ref>PMID:16143459</ref>
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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Prokaryotic viruses have evolved various mechanisms to transport their genomes across bacterial cell walls. Many bacteriophages use a tail to perform this function, whereas tail-less phages rely on host organelles. However, the tail-less, icosahedral, single-stranded DNA PhiX174-like coliphages do not fall into these well-defined infection processes. For these phages, DNA delivery requires a DNA pilot protein. Here we show that the PhiX174 pilot protein H oligomerizes to form a tube whose function is most probably to deliver the DNA genome across the host's periplasmic space to the cytoplasm. The 2.4 A resolution crystal structure of the in vitro assembled H protein's central domain consists of a 170 A-long alpha-helical barrel. The tube is constructed of ten alpha-helices with their amino termini arrayed in a right-handed super-helical coiled-coil and their carboxy termini arrayed in a left-handed super-helical coiled-coil. Genetic and biochemical studies demonstrate that the tube is essential for infectivity but does not affect in vivo virus assembly. Cryo-electron tomograms show that tubes span the periplasmic space and are present while the genome is being delivered into the host cell's cytoplasm. Both ends of the H protein contain transmembrane domains, which anchor the assembled tubes into the inner and outer cell membranes. The central channel of the H-protein tube is lined with amide and guanidinium side chains. This may be a general property of viral DNA conduits and is likely to be critical for efficient genome translocation into the host.
 
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Icosahedral bacteriophage PhiX174 forms a tail for DNA transport during infection.,Sun L, Young LN, Zhang X, Boudko SP, Fokine A, Zbornik E, Roznowski AP, Molineux IJ, Rossmann MG, Fane BA Nature. 2013 Dec 15. doi: 10.1038/nature12816. PMID:24336205<ref>PMID:24336205</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 4jpp" style="background-color:#fffaf0;"></div>
 
== References ==
== References ==
<references/>
<references/>

Current revision

Bacteriophage phiX174 H protein residues 143-282

PDB ID 4jpp

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