View source for 7kwy


==X-ray Crystal Structure of PlyCB Mutant R66K==
<StructureSection load='7kwy' size='340' side='right'caption='[[7kwy]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7kwy]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_virus_C1 Streptococcus virus C1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7KWY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7KWY 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]] 1.7&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</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=7kwy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7kwy OCA], [https://pdbe.org/7kwy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7kwy RCSB], [https://www.ebi.ac.uk/pdbsum/7kwy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7kwy ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q7Y3F3_9CAUD Q7Y3F3_9CAUD] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Endolysin enzymes from bacteriophage cause bacterial lysis by degrading the peptidoglycan cell wall. The streptococcal C1 phage endolysin PlyC, is the most potent endolysin described to date and can rapidly lyse group A, C, and E streptococci. PlyC is known to bind the Group A streptococcal cell wall, but the specific molecular target or the binding site within PlyC remain uncharacterized. Here we report for the first time, that the polyrhamnose backbone of the Group A streptococcal cell wall is the binding target of PlyC. We have also characterized the putative rhamnose binding groove of PlyC and found four key residues that were critical to either the folding or the cell wall binding action of PlyC. Based on our results, we suggest that the interaction between PlyC and the cell wall may not be a high-affinity interaction as previously proposed, but rather a high avidity one, allowing for PlyC's remarkable lytic activity. Resistance to our current antibiotics is reaching crisis levels and there is an urgent need to develop the antibacterial agents with new modes of action. A detailed understanding of this potent endolysin may facilitate future developments of PlyC as a tool against the rise of antibiotic resistance.

High avidity drives the interaction between the streptococcal C1 phage endolysin, PlyC, with the cell surface carbohydrates of Group A Streptococcus.,Broendum SS, Williams DE, Hayes BK, Kraus F, Fodor J, Clifton BE, Geert Volbeda A, Codee JDC, Riley BT, Drinkwater N, Farrow KA, Tsyganov K, Heselpoth RD, Nelson DC, Jackson CJ, Buckle AM, McGowan S Mol Microbiol. 2021 Mar 23. doi: 10.1111/mmi.14719. PMID:33756056<ref>PMID:33756056</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7kwy" style="background-color:#fffaf0;"></div>

==See Also==
*[[Lysin 3D structures|Lysin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Streptococcus virus C1]]
[[Category: Broendum SS]]
[[Category: Drinkwater N]]
[[Category: Hayes BK]]
[[Category: McGowan S]]
[[Category: Williams DE]]