View source for 4le7


==The Crystal Structure of Pyocin L1 at 2.09 Angstroms==
<StructureSection load='4le7' size='340' side='right'caption='[[4le7]], [[Resolution|resolution]] 2.09&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4le7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa_str._C_1433 Pseudomonas aeruginosa str. C 1433]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LE7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LE7 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]] 2.09&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></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=4le7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4le7 OCA], [https://pdbe.org/4le7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4le7 RCSB], [https://www.ebi.ac.uk/pdbsum/4le7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4le7 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/T2LG16_PSEAI T2LG16_PSEAI] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Lectin-like bacteriocins consist of tandem monocot mannose-binding domains and display a genus-specific killing activity. Here we show that pyocin L1, a novel member of this family from Pseudomonas aeruginosa, targets susceptible strains of this species through recognition of the common polysaccharide antigen (CPA) of P. aeruginosa lipopolysaccharide that is predominantly a homopolymer of d-rhamnose. Structural and biophysical analyses show that recognition of CPA occurs through the C-terminal carbohydrate-binding domain of pyocin L1 and that this interaction is a prerequisite for bactericidal activity. Further to this, we show that the previously described lectin-like bacteriocin putidacin L1 shows a similar carbohydrate-binding specificity, indicating that oligosaccharides containing d-rhamnose and not d-mannose, as was previously thought, are the physiologically relevant ligands for this group of bacteriocins. The widespread inclusion of d-rhamnose in the lipopolysaccharide of members of the genus Pseudomonas explains the unusual genus-specific activity of the lectin-like bacteriocins.

Lectin-Like Bacteriocins from Pseudomonas spp. Utilise D-Rhamnose Containing Lipopolysaccharide as a Cellular Receptor.,McCaughey LC, Grinter R, Josts I, Roszak AW, Waloen KI, Cogdell RJ, Milner J, Evans T, Kelly S, Tucker NP, Byron O, Smith B, Walker D PLoS Pathog. 2014 Feb 6;10(2):e1003898. doi: 10.1371/journal.ppat.1003898., eCollection 2014 Feb. PMID:24516380<ref>PMID:24516380</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4le7" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pseudomonas aeruginosa str. C 1433]]
[[Category: Cogdell RJ]]
[[Category: Grinter R]]
[[Category: Mccaughey L]]
[[Category: Roszak AW]]
[[Category: Walker D]]