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| ==Bacteriophage phiX174 H protein residues 143-282== | | ==Bacteriophage phiX174 H protein residues 143-282== |
- | <StructureSection load='4jpp' size='340' side='right' caption='[[4jpp]], [[Resolution|resolution]] 2.40Å' scene=''> | + | <StructureSection load='4jpp' size='340' side='right'caption='[[4jpp]], [[Resolution|resolution]] 2.40Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[4jpp]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Bpphx Bpphx]. 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 [http://oca.weizmann.ac.il/oca-docs/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> |
- | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4jpn|4jpn]]</td></tr> | + | </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> |
- | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">H ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10847 BPPHX])</td></tr>
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- | <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=4jpp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jpp OCA], [http://pdbe.org/4jpp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4jpp RCSB], [http://www.ebi.ac.uk/pdbsum/4jpp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4jpp ProSAT]</span></td></tr> | + | |
| </table> | | </table> |
| == Function == | | == Function == |
- | [[http://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> |
| <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
- | [[Category: Bpphx]] | + | [[Category: Escherichia virus phiX174]] |
- | [[Category: Boudko, S B]] | + | [[Category: Large Structures]] |
- | [[Category: Fane, B A]] | + | [[Category: Boudko SB]] |
- | [[Category: Fokine, A]] | + | [[Category: Fane BA]] |
- | [[Category: Rossmann, M G]] | + | [[Category: Fokine A]] |
- | [[Category: Sun, L]] | + | [[Category: Rossmann MG]] |
- | [[Category: Young, L N]] | + | [[Category: Sun L]] |
- | [[Category: Zhang, X]] | + | [[Category: Young LN]] |
- | [[Category: Helical barrel]]
| + | [[Category: Zhang X]] |
- | [[Category: Pilot dna during phage infection]]
| + | |
- | [[Category: Tail tube]]
| + | |
- | [[Category: Viral protein]]
| + | |
| Structural highlights
Function
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.[1] [2]
Publication Abstract from PubMed
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.
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[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Inagaki M, Tanaka A, Suzuki R, Wakashima H, Kawaura T, Karita S, Nishikawa S, Kashimura N. Characterization of the binding of spike H protein of bacteriophage phiX174 with receptor lipopolysaccharides. J Biochem. 2000 Apr;127(4):577-83. PMID:10739948
- ↑ Inagaki M, Wakashima H, Kato M, Kaitani K, Nishikawa S. Crucial role of the lipid part of lipopolysaccharide for conformational change of minor spike H protein of bacteriophage phiX174. FEMS Microbiol Lett. 2005 Oct 15;251(2):305-11. PMID:16143459 doi:http://dx.doi.org/10.1016/j.femsle.2005.08.014
- ↑ Sun L, Young LN, Zhang X, Boudko SP, Fokine A, Zbornik E, Roznowski AP, Molineux IJ, Rossmann MG, Fane BA. Icosahedral bacteriophage PhiX174 forms a tail for DNA transport during infection. Nature. 2013 Dec 15. doi: 10.1038/nature12816. PMID:24336205 doi:http://dx.doi.org/10.1038/nature12816
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