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5w6f

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Current revision (14:14, 13 March 2024) (edit) (undo)
 
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<StructureSection load='5w6f' size='340' side='right'caption='[[5w6f]], [[Resolution|resolution]] 2.18&Aring;' scene=''>
<StructureSection load='5w6f' size='340' side='right'caption='[[5w6f]], [[Resolution|resolution]] 2.18&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5w6f]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5W6F OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5W6F FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5w6f]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_virus_CBA120 Escherichia virus CBA120]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5W6F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5W6F 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=CL:CHLORIDE+ION'>CL</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]] 2.18&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5w6s|5w6s]], [[5w6p|5w6p]]</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=CL:CHLORIDE+ION'>CL</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=5w6f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5w6f OCA], [http://pdbe.org/5w6f PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5w6f RCSB], [http://www.ebi.ac.uk/pdbsum/5w6f PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5w6f ProSAT]</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=5w6f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5w6f OCA], [https://pdbe.org/5w6f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5w6f RCSB], [https://www.ebi.ac.uk/pdbsum/5w6f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5w6f 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/G3M191_9CAUD G3M191_9CAUD]
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Bacteriophages recognize their host cells with the help of tail fiber and tailspike proteins that bind, cleave, or modify certain structures on the cell surface. The spectrum of ligands to which the tail fibers and tailspikes can bind is the primary determinant of the host range. Bacteriophages with multiple tailspike/tail fibers are thought to have a wider host range than their less endowed relatives but the function of these proteins remains poorly understood. Here, we describe the structure, function, and substrate specificity of three tailspike proteins of bacteriophage CBA120-TSP2, TSP3 and TSP4 (orf211 through orf213, respectively). We show that tailspikes TSP2, TSP3 and TSP4 are hydrolases that digest the O157, O77, and O78 Escherichia coli O-antigens, respectively. We demonstrate that recognition of the E. coli O157:H7 host by CBA120 involves binding to and digesting the O157 O-antigen by TSP2. We report the crystal structure of TSP2 in complex with a repeating unit of the O157 O-antigen. We demonstrate that according to the specificity of its tailspikes TSP2, TSP3, and TSP4, CBA120 can infect E. coli O157, O77, and O78, respectively. We also show that CBA120 infects Salmonella enterica serovar Minnesota, and this host range expansion is likely due to the function of TSP1. Finally, we describe the assembly pathway and the architecture of the TSP1-TSP2-TSP3-TSP4 branched complex in CBA120 and its related ViI-like phages.
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Structure and Function of the Branched Receptor-Binding Complex of Bacteriophage CBA120.,Plattner M, Shneider MM, Arbatsky NP, Shashkov AS, Chizhov AO, Nazarov S, Prokhorov NS, Taylor NMI, Buth SA, Gambino M, Gencay YE, Brondsted L, Kutter EM, Knirel YA, Leiman PG J Mol Biol. 2019 Sep 6;431(19):3718-3739. doi: 10.1016/j.jmb.2019.07.022. Epub, 2019 Jul 17. PMID:31325442<ref>PMID:31325442</ref>
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==See Also==
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*[[Tailspike protein 3D structures|Tailspike protein 3D structures]]
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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 5w6f" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Escherichia virus CBA120]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Leiman, P G]]
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[[Category: Leiman PG]]
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[[Category: Plattner, M]]
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[[Category: Plattner M]]
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[[Category: Shneider, M M]]
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[[Category: Shneider MM]]
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[[Category: Cba120]]
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[[Category: Hydrolase]]
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[[Category: Tailspike]]
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[[Category: Viral protein]]
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Current revision

Crystal structure of Bacteriophage CBA120 tailspike protein 3 (TSP3, orf212)

PDB ID 5w6f

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