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| | <StructureSection load='2f0c' size='340' side='right'caption='[[2f0c]], [[Resolution|resolution]] 1.65Å' scene=''> | | <StructureSection load='2f0c' size='340' side='right'caption='[[2f0c]], [[Resolution|resolution]] 1.65Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2f0c]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacteriophage_tp901-1 Bacteriophage tp901-1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2F0C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2F0C FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2f0c]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Lactococcus_phage_TP901-1 Lactococcus phage TP901-1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2F0C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2F0C FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.65Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2bsd|2bsd]], [[1zru|1zru]], [[2bse|2bse]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ORF49/bbp ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=35345 Bacteriophage TP901-1])</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=2f0c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2f0c OCA], [https://pdbe.org/2f0c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2f0c RCSB], [https://www.ebi.ac.uk/pdbsum/2f0c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2f0c 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=2f0c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2f0c OCA], [https://pdbe.org/2f0c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2f0c RCSB], [https://www.ebi.ac.uk/pdbsum/2f0c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2f0c ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q9G096_9CAUD Q9G096_9CAUD] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacteriophage tp901-1]] | + | [[Category: Lactococcus phage TP901-1]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Cambillau, C]] | + | [[Category: Cambillau C]] |
| - | [[Category: Spinelli, S]] | + | [[Category: Spinelli S]] |
| - | [[Category: Helix parallel bundle]]
| + | |
| - | [[Category: Beta prism]]
| + | |
| - | [[Category: Beta-barrel]]
| + | |
| - | [[Category: Viral protein]]
| + | |
| Structural highlights
Function
Q9G096_9CAUD
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Lactococcus lactis is a gram-positive bacterium widely used by the dairy industry. Several industrial L. lactis strains are sensitive to various distinct bacteriophages. Most of them belong to the Siphoviridae family and comprise several species, among which the 936 and P335 are prominent. Members of these two phage species recognize their hosts through the interaction of their receptor-binding protein (RBP) with external cell wall saccharidices of the host, the "receptors." We report here the 1.65 A resolution crystal structure of the RBP from phage TP901-1, a member of the P335 species. This RBP of 163 amino acids is a homotrimer comprising three domains: a helical N terminus, an interlaced beta-prism, and a beta-barrel, the head domain (residues 64-163), which binds a glycerol molecule. Fluorescence quenching experiments indicated that the RBP exhibits high affinity for glycerol, muramyl-dipeptide, and other saccharides in solution. The structural comparison of this RBP with that of lactococcal phage p2 RBP, a member of the 936 species (Spinelli, S., Desmyter, A., Verrips, C. T., de Haard, J. W., Moineau, S., and Cambillau, C. (2006) Nat. Struct. Mol. Biol. 13, 85-89) suggests a large extent of modularity in RBPs of lactococcal phages.
Modular structure of the receptor binding proteins of Lactococcus lactis phages. The RBP structure of the temperate phage TP901-1.,Spinelli S, Campanacci V, Blangy S, Moineau S, Tegoni M, Cambillau C J Biol Chem. 2006 May 19;281(20):14256-62. Epub 2006 Mar 20. PMID:16549427[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Spinelli S, Campanacci V, Blangy S, Moineau S, Tegoni M, Cambillau C. Modular structure of the receptor binding proteins of Lactococcus lactis phages. The RBP structure of the temperate phage TP901-1. J Biol Chem. 2006 May 19;281(20):14256-62. Epub 2006 Mar 20. PMID:16549427 doi:10.1074/jbc.M600666200
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