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3da0
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 3da0 is ON HOLD Authors: Siponen, M.I., Blangy, S., Spinelli, S., Vera, L., Cambillau, C., Campanacci, V. Description: Crystal structure of a cleav...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of a cleaved form of a chimeric receptor binding protein from Lactococcal phages subspecies TP901-1 and p2== | |
| + | <StructureSection load='3da0' size='340' side='right'caption='[[3da0]], [[Resolution|resolution]] 1.65Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3da0]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Lactococcus_phage_TP901-1 Lactococcus phage TP901-1] and [https://en.wikipedia.org/wiki/Lactococcus_virus_P2 Lactococcus virus P2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3DA0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3DA0 FirstGlance]. <br> | ||
| + | </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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3da0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3da0 OCA], [https://pdbe.org/3da0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3da0 RCSB], [https://www.ebi.ac.uk/pdbsum/3da0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3da0 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/Q9G096_9CAUD Q9G096_9CAUD] [https://www.uniprot.org/uniprot/RBP_BPLP2 RBP_BPLP2] Binds to the host phosphopolysaccharides at the onset of infection. Upon activation by calcium, the receptor binding proteins change their conformation, presenting their binding sites to the host, and a channel opens at the bottom of the baseplate for DNA ejection.<ref>PMID:20351260</ref> <ref>PMID:24027307</ref> | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/da/3da0_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3da0 ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Lactococcus lactis, a gram-positive bacterium widely used by the dairy industry to manufacture cheeses, is subject to infection by a diverse population of virulent phages. We have previously determined the structures of three receptor binding proteins (RBPs) from lactococcal phages TP901-1, p2, and bIL170, each of them having a distinct host range. Virulent phages p2 and bIL170 are classified within the 936 group, while the temperate phage TP901-1 is a member of the genetically distinct P335 polythetic group. These RBPs comprise three domains: the N-terminal domain, binding to the virion particle; a beta-helical linker domain; and the C-terminal domain, bearing the receptor binding site used for host recognition. Here, we have designed, expressed, and determined the structure of an RBP chimera in which the N-terminal and linker RBP domains of phage TP901-1 (P335) are fused to the C-terminal RBP domain of phage p2 (936). This chimera exhibits a stable structure that closely resembles the parental structures, while a slight displacement of the linker made RBP domain adaptation efficient. The receptor binding site is structurally indistinguishable from that of native p2 RBP and binds glycerol with excellent affinity. | ||
| - | + | Crystal structure of a chimeric receptor binding protein constructed from two lactococcal phages.,Siponen M, Spinelli S, Blangy S, Moineau S, Cambillau C, Campanacci V J Bacteriol. 2009 May;191(10):3220-5. Epub 2009 Mar 13. PMID:19286807<ref>PMID:19286807</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 3da0" style="background-color:#fffaf0;"></div> | |
| - | + | == References == | |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Lactococcus phage TP901-1]] | ||
| + | [[Category: Lactococcus virus P2]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Blangy S]] | ||
| + | [[Category: Cambillau C]] | ||
| + | [[Category: Campanacci V]] | ||
| + | [[Category: Siponen MI]] | ||
| + | [[Category: Spinelli S]] | ||
| + | [[Category: Vera L]] | ||
Current revision
Crystal structure of a cleaved form of a chimeric receptor binding protein from Lactococcal phages subspecies TP901-1 and p2
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