3aqj

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<StructureSection load='3aqj' size='340' side='right'caption='[[3aqj]], [[Resolution|resolution]] 1.27&Aring;' scene=''>
<StructureSection load='3aqj' size='340' side='right'caption='[[3aqj]], [[Resolution|resolution]] 1.27&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3aqj]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Bpp2 Bpp2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AQJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3AQJ FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3aqj]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_virus_P2 Escherichia virus P2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AQJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3AQJ 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=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</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]] 1.27&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">V ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10679 BPP2])</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=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</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=3aqj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3aqj OCA], [https://pdbe.org/3aqj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3aqj RCSB], [https://www.ebi.ac.uk/pdbsum/3aqj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3aqj 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=3aqj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3aqj OCA], [https://pdbe.org/3aqj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3aqj RCSB], [https://www.ebi.ac.uk/pdbsum/3aqj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3aqj ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/VPV_BPP2 VPV_BPP2]] Forms the small spike at the tip of the tail.
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[https://www.uniprot.org/uniprot/SPIKE_BPP2 SPIKE_BPP2] Forms the small spikes on the baseplate that plug the end of the tube before DNA ejection and form a channel perforating the host membrane during ejection. Involved in baseplate assembly.<ref>PMID:21821878</ref> <ref>PMID:22325780</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The adsorption and infection of bacteriophage P2 is mediated by tail fibres and tail spikes. The tail spikes on the tail baseplate are used to irreversibly adsorb to the host cells. Recently, a P2 phage tail-spike protein, gpV, was purified and it was shown that a C-terminal domain, Ser87-Leu211, is sufficient for the binding of gpV to host Escherichia coli membranes [Kageyama et al. (2009), Biochemistry, 48, 10129-10135]. In this paper, the crystal structure of the C-terminal domain of P2 gpV is reported. The structure is a triangular pyramid and looks like a spearhead composed of an intertwined beta-sheet, a triple beta-helix and a metal-binding region containing iron, calcium and chloride ions.
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The host-binding domain of the P2 phage tail spike reveals a trimeric iron-binding structure.,Yamashita E, Nakagawa A, Takahashi J, Tsunoda K, Yamada S, Takeda S Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Aug 1;67(Pt 8):837-41., Epub 2011 Jul 13. PMID:21821878<ref>PMID:21821878</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 3aqj" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
*[[Sandbox 3001|Sandbox 3001]]
*[[Sandbox 3001|Sandbox 3001]]
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*[[Spike protein|Spike protein]]
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*[[Spike protein 3D structures|Spike protein 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Bpp2]]
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[[Category: Escherichia virus P2]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Nakagawa, A]]
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[[Category: Nakagawa A]]
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[[Category: Takeda, S]]
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[[Category: Takeda S]]
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[[Category: Yamashita, E]]
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[[Category: Yamashita E]]
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[[Category: Bacteriophage]]
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[[Category: Beta-helix]]
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[[Category: Infection]]
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[[Category: Iron binding]]
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[[Category: Metal binding protein]]
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[[Category: Tail spike]]
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Current revision

Crystal Structure of a C-terminal domain of the bacteriophage P2 tail spike protein, gpV

PDB ID 3aqj

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