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3qay

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Catalytic domain of CD27L endolysin targeting Clostridia Difficile

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Retrieved from "http://52.214.119.220/wiki/index.php/3qay"

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 <StructureSection load='3qay' size='340' side='right'caption='[[3qay]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3qay]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridium_bacteriophage_phicd27 Clostridium bacteriophage phicd27]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QAY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QAY FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3qay]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridium_virus_phiCD27 Clostridium virus phiCD27]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QAY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QAY FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 2&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=3qay FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qay OCA], [https://pdbe.org/3qay PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qay RCSB], [https://www.ebi.ac.uk/pdbsum/3qay PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qay ProSAT]</span></td></tr>
 </table>
-<div style="background-color:#fffaf0;">
+== Function ==
-== Publication Abstract from PubMed ==
+[https://www.uniprot.org/uniprot/B6SBV8_9CAUD B6SBV8_9CAUD]
-Endolysin CD27L causes cell lysis of the pathogen Clostridium difficile, a major cause of nosocomial infection. We report a structural and functional analysis of the catalytic activity of CD27L against C. difficile and other bacterial strains. We show that truncation of the endolysin to the N-terminal domain, CD27L1-179, gave an increased lytic activity against cells of C. difficile, while the C-terminal region, CD27L180-270, failed to produce lysis. CD27L1-179 also has increased activity against other bacterial species that are targeted by the full-length protein and in addition was able to lyse some CD27L-insensitive strains. However, CD27L1-179 retained a measure of specificity, failing to lyse a wide range of bacteria. The use of green fluorescent protein (GFP)-labeled proteins demonstrated that both CD27L and CD27L1-179 bound to C. difficile cell walls. The crystal structure of CD27L1-179 confirms that the enzyme is a zinc-dependent N-acetylmuramoyl-l-alanine amidase. A structure-based sequence analysis allowed us to identify four catalytic residues, a proton relay cascade, and a substrate binding pocket. A BLAST search shows that the closest-related amidases almost exclusively target Clostridia. This implied that the catalytic domain alone contained features that target a specific bacterial species. To test this hypothesis, we modified Leu 98 to a Trp residue which is found in an endolysin from a bacteriophage of Listeria monocytogenes (PlyPSA). This mutation in CD27L resulted in an increased activity against selected serotypes of L. monocytogenes, demonstrating the potential to tune the species specificity of the catalytic domain of an endolysin.
-Structure-based modification of a Clostridium difficile-targeting endolysin affects activity and host range.,Mayer MJ, Garefalaki V, Spoerl R, Narbad A, Meijers R J Bacteriol. 2011 Oct;193(19):5477-86. Epub 2011 Jul 29. PMID:21803993<ref>PMID:21803993</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 3qay" style="background-color:#fffaf0;"></div>
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Clostridium bacteriophage phicd27]]
+[[Category: Clostridium virus phiCD27]]
 [[Category: Large Structures]]
-[[Category: Garefaliki, V]]
+[[Category: Garefaliki V]]
-[[Category: Mayer, M J]]
+[[Category: Mayer MJ]]
-[[Category: Meijers, R]]
+[[Category: Meijers R]]
-[[Category: Narbad, A]]
+[[Category: Narbad A]]
-[[Category: Spoerl, R]]
+[[Category: Spoerl R]]
-[[Category: Amidase a/b fold]]
-[[Category: Lyase]]

3qay

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Catalytic domain of CD27L endolysin targeting Clostridia Difficile

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