3th0: Difference between revisions

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 <StructureSection load='3th0' size='340' side='right'caption='[[3th0]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3th0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bpp22 Bpp22]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TH0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TH0 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3th0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmonella_virus_P22 Salmonella virus P22]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TH0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TH0 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>, <scene name='pdbligand=GLA:ALPHA+D-GALACTOSE'>GLA</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=RAM:ALPHA-L-RHAMNOSE'>RAM</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]] 1.75&#8491;</td></tr>
-<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=PZU:3,6-DIDEOXY-ALPHA-D-RIBO-HEXOPYRANOSE'>PZU</scene></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLA:ALPHA+D-GALACTOSE'>GLA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=PZU:3,6-DIDEOXY-ALPHA-D-RIBO-HEXOPYRANOSE'>PZU</scene>, <scene name='pdbligand=RAM:ALPHA-L-RHAMNOSE'>RAM</scene></td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1tyv|1tyv]], [[1tyx|1tyx]], [[1tyu|1tyu]]</div></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">9, phage p22 gene 9 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10754 BPP22])</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=3th0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3th0 OCA], [https://pdbe.org/3th0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3th0 RCSB], [https://www.ebi.ac.uk/pdbsum/3th0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3th0 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/TSPE_BPP22 TSPE_BPP22]] Non-covalently bound to the neck of the phage capsid and mediating attachment of the viral particle to host cell-surface polysaccharide. It displays endorhamnosidase enzymatic activity, hydrolyzing the alpha-1,3-O-glycosidic linkage between rhamnose and galactose of the O-antigen polysaccharide.<ref>PMID:12837775</ref> <ref>PMID:20817910</ref>
+[https://www.uniprot.org/uniprot/FIBER_BPP22 FIBER_BPP22] Structural component of the short non-contractile tail. The tail comprises six fibers that mediate primary attachment to the host cell lipopolysaccharides (LPS) and display endorhamnosidase enzymatic activity, hydrolyzing the alpha-1,3-O-glycosidic linkage between rhamnose and galactose of the O-antigen polysaccharide. Digestion of the LPS brings the capsid near the cell outer membrane.<ref>PMID:12837775</ref> <ref>PMID:20817910</ref>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-Bacteriophage P22 recognizes O-antigen polysaccharides of Salmonella enterica subsp. enterica (S.) with its tailspike protein (TSP). In the serovars S. Typhimurium, S. Enteritidis, and S. Paratyphi A, the tetrasaccharide repeat units of the respective O-antigens consist of an identical main chain trisaccharide but different 3,6-dideoxyhexose substituents. Here, the epimers abequose, tyvelose and paratose determine the specific serotype. P22 TSP recognizes O-antigen octasaccharides in an extended binding site with a single 3,6-dideoxyhexose binding pocket. We have isolated S. Paratyphi A octasaccharides which were not available previously and determined the crystal structure of their complex with P22 TSP. We discuss our data together with crystal structures of complexes with S. Typhimurium and S. Enteritidis octasaccharides determined earlier. Isothermal titration calorimetry showed that S. Paratyphi A octasaccharide binds P22 TSP less tightly, with a difference in binding free energy of approximately 7 kJ mol(-1) at 20 degrees C compared with S. Typhimurium and S. Enteritidis octasaccharides. Individual protein-carbohydrate contacts were probed by amino acid replacements showing that the dideoxyhexose pocket contributes to binding of all three serotypes. However, S. Paratyphi A octasaccharides bind in a conformation with an energetically unfavorable varphi/psi glycosidic bond angle combination. In contrast, octasaccharides from the other serotypes bind as solution-like conformers. Two water molecules are conserved in all P22 TSP complexes with octasaccharides of different serotypes. They line the dideoxyhexose binding pocket and force the S. Paratyphi A octasaccharides to bind as nonsolution conformers. This emphasizes the role of solvent as part of carbohydrate binding sites.
-An essential serotype recognition pocket on phage P22 tailspike protein forces Salmonella enterica serovar Paratyphi A O-antigen fragments to bind as nonsolution conformers.,Andres D, Gohlke U, Broeker NK, Schulze S, Rabsch W, Heinemann U, Barbirz S, Seckler R Glycobiology. 2013 Apr;23(4):486-94. doi: 10.1093/glycob/cws224. Epub 2013 Jan 3. PMID:23292517<ref>PMID:23292517</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 3th0" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[Tailspike protein|Tailspike protein]]
+*[[Tailspike protein 3D structures|Tailspike protein 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Bpp22]]
 [[Category: Large Structures]]
-[[Category: Andres, D]]
+[[Category: Salmonella virus P22]]
-[[Category: Barbirz, S]]
+[[Category: Andres D]]
-[[Category: Gohlke, U]]
+[[Category: Barbirz S]]
-[[Category: Heinemann, U]]
+[[Category: Gohlke U]]
-[[Category: Seckler, R]]
+[[Category: Heinemann U]]
-[[Category: Bacteriophage p22 baseplate]]
+[[Category: Seckler R]]
-[[Category: Beta helix]]
-[[Category: Binding protein lipopolysaccharide]]
-[[Category: Carbohydrate]]
-[[Category: Cell receptor]]
-[[Category: Endoglycosidase]]
-[[Category: Host recognition]]
-[[Category: Hydrolase]]
-[[Category: Receptor]]
-[[Category: Recognition]]
-[[Category: Viral adhesion protein]]
-[[Category: Viral protein]]