3shs

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==Three N-terminal domains of the bacteriophage RB49 Highly Immunogenic Outer Capsid protein (Hoc)==
==Three N-terminal domains of the bacteriophage RB49 Highly Immunogenic Outer Capsid protein (Hoc)==
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<StructureSection load='3shs' size='340' side='right' caption='[[3shs]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
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<StructureSection load='3shs' size='340' side='right'caption='[[3shs]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3shs]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_rb49 Enterobacteria phage rb49]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SHS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3SHS FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3shs]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_phage_RB49 Escherichia phage RB49]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SHS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SHS FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 1.951&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">hoc ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=50948 Enterobacteria phage RB49])</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=MG:MAGNESIUM+ION'>MG</scene></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=3shs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3shs OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3shs RCSB], [http://www.ebi.ac.uk/pdbsum/3shs PDBsum]</span></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=3shs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3shs OCA], [https://pdbe.org/3shs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3shs RCSB], [https://www.ebi.ac.uk/pdbsum/3shs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3shs 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/Q7Y442_BPRB4 Q7Y442_BPRB4]
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The head of bacteriophage T4 is decorated with 155 copies of the highly antigenic outer capsid protein or Hoc. One Hoc molecule binds near the center of each hexameric capsomer. Hoc is dispensable for capsid assembly and has been used to display pathogenic antigens on the T4 surface. Here we report the crystal structure of a protein containing the first three of four domains of Hoc from the bacteriophage RB49, a close relative of T4. The structure shows an approximately linear arrangement of the protein domains. Each of these domains has an immunoglobulin-like fold, frequently found in cell attachment molecules. In addition we report biochemical data suggesting that Hoc can bind to E. coli supporting the hypothesis that Hoc could attach the phage capsids to bacterial surfaces and maybe also to other organisms. The ability of such reversible adhesion probably provides survival advantages to the bacteriophage.
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Structure of the Three N-terminal Immunoglobulin Domains of the Highly Immunogenic Outer Capsid Protein from a T4-like Bacteriophage.,Fokine A, Islam MZ, Zhang Z, Bowman VD, Rao VB, Rossmann MG J Virol. 2011 Jun 1. PMID:21632759<ref>PMID:21632759</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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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Enterobacteria phage rb49]]
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[[Category: Escherichia phage RB49]]
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[[Category: Bowman, V D]]
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[[Category: Large Structures]]
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[[Category: Fokine, A]]
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[[Category: Bowman VD]]
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[[Category: Islam, M Z]]
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[[Category: Fokine A]]
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[[Category: Rao, V B]]
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[[Category: Islam MZ]]
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[[Category: Rossmann, M G]]
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[[Category: Rao VB]]
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[[Category: Zhang, Z]]
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[[Category: Rossmann MG]]
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[[Category: Bacterial surface]]
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[[Category: Zhang Z]]
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[[Category: Bacteriophage surface]]
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[[Category: E coli surface]]
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[[Category: Immunoglobulin-like domain]]
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[[Category: Interaction with bacteria]]
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[[Category: Phage capsid decorative protein]]
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[[Category: Viral protein]]
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[[Category: Virus surface]]
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Current revision

Three N-terminal domains of the bacteriophage RB49 Highly Immunogenic Outer Capsid protein (Hoc)

PDB ID 3shs

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