5ly8

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<StructureSection load='5ly8' size='340' side='right'caption='[[5ly8]], [[Resolution|resolution]] 1.28&Aring;' scene=''>
<StructureSection load='5ly8' size='340' side='right'caption='[[5ly8]], [[Resolution|resolution]] 1.28&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5ly8]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Lactobacillus_phage_j-1 Lactobacillus phage j-1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LY8 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5LY8 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5ly8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Lactobacillus_phage_J-1 Lactobacillus phage J-1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LY8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5LY8 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=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]] 1.28&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">J1_16 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1414736 Lactobacillus phage J-1])</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://proteopedia.org/fgij/fg.htm?mol=5ly8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ly8 OCA], [http://pdbe.org/5ly8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ly8 RCSB], [http://www.ebi.ac.uk/pdbsum/5ly8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ly8 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=5ly8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ly8 OCA], [https://pdbe.org/5ly8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ly8 RCSB], [https://www.ebi.ac.uk/pdbsum/5ly8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ly8 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/U5U3S0_9CAUD U5U3S0_9CAUD]
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Bacteriophage replication requires specific host-recognition. Some siphophages harbour a large complex, the baseplate, at the tip of their non-contractile tail. This baseplate holds receptor binding proteins (RBPs) that can recognize the host cell-wall polysaccharide (CWPS) and specifically attach the phage to its host. While most phages possess a dedicated RBP, the phage J-1 that infects Lactobacillus casei seemed to lack one. It has been shown that the phage J-1 distal tail protein (Dit) plays a role in host recognition and that its sequence comprises two inserted modules compared with 'classical' Dits. The first insertion is similar to carbohydrate-binding modules (CBMs), whereas the second insertion remains undocumented. Here, we determined the structure of the second insertion and found it also similar to several CBMs. Expressed insertion CBM2, but not CBM1, binds to L. casei cells and neutralize phage attachment to the bacterial cell wall and the isolated and purified CWPS of L. casei BL23 prevents CBM2 attachment to the host. Electron microscopy single particle reconstruction of the J-1 virion baseplate revealed that CBM2 is projected at the periphery of Dit to optimally bind the CWPS receptor. Taken together, these results identify J-1 evolved Dit as the phage RBP.
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Evolved distal tail carbohydrate binding modules of Lactobacillus phage J-1: a novel type of anti-receptor widespread among lactic acid bacteria phages.,Dieterle ME, Spinelli S, Sadovskaya I, Piuri M, Cambillau C Mol Microbiol. 2017 Feb 14. doi: 10.1111/mmi.13649. PMID:28196397<ref>PMID:28196397</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 5ly8" 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: Lactobacillus phage j-1]]
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[[Category: Lactobacillus phage J-1]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Cambillau, C]]
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[[Category: Cambillau C]]
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[[Category: Dieterle, M E]]
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[[Category: Dieterle M-E]]
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[[Category: Piuri, M]]
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[[Category: Piuri M]]
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[[Category: Spinelli, S]]
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[[Category: Spinelli S]]
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[[Category: Bacteriophage infection]]
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[[Category: Carbohydrate binding module]]
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[[Category: Fluorescence microscopy]]
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[[Category: Lactobacillus casei]]
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[[Category: Sugar binding protein]]
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Current revision

Structure of the CBM2 module of Lactobacillus casei BL23 phage J-1 evolved Dit.

PDB ID 5ly8

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