View source for 4krt


==X-ray structure of endolysin from clostridium perfringens phage phiSM101==
<StructureSection load='4krt' size='340' side='right'caption='[[4krt]], [[Resolution|resolution]] 1.92&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4krt]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridium_phage_phiSM101 Clostridium phage phiSM101]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KRT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4KRT 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]] 1.92&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=MLA:MALONIC+ACID'>MLA</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=4krt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4krt OCA], [https://pdbe.org/4krt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4krt RCSB], [https://www.ebi.ac.uk/pdbsum/4krt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4krt ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q0SPG7_9CAUD Q0SPG7_9CAUD] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Gram-positive bacteria possess a thick cell wall composed of a mesh polymer of peptidoglycans, which provides physical protection. Endolysins encoded by phages infecting bacteria can hydrolyse peptidoglycans in the bacterial cell wall, killing the host bacteria immediately. The endolysin (Psm) encoded by episomal phage phiSM101 of enterotoxigenic Clostridium perfringens type A strain SM101 exhibits potent lytic activity towards most strains of Clostridium perfringens. Psm has an N-terminal catalytic domain highly homologous to N-acetylmuramidases belonging to the glycoside hydrolase 25 family, and C-terminal tandem repeated bacterial Src homology 3 (SH3_3) domains as the cell wall-binding domain. The X-ray structure of full-length Psm and a catalytic domain of Psm in complex with N-acetylglucosamine were determined to elucidate the catalytic reaction and cell wall recognition mechanisms of Psm. The results showed that Psm may have adopted a neighbouring-group mechanism for the catalytic hydrolysing reaction in which the N-acetyl carbonyl group of the substrate was involved in the formation of an oxazolinium ion intermediate. Based on structural comparisons with other endolysins and a modelling study, we proposed that tandem repeated SH3_3 domains of Psm recognized the peptide side-chains of peptidoglycans to assist the catalytic domain hydrolysing the glycan backbone.

X-ray structure of a novel endolysin encoded by episomal phage phiSM101 of Clostridium perfringens.,Tamai E, Yoshida H, Sekiya H, Nariya H, Miyata S, Okabe A, Kuwahara T, Maki J, Kamitori S Mol Microbiol. 2014 Apr;92(2):326-37. doi: 10.1111/mmi.12559. Epub 2014 Mar 5. PMID:24674022<ref>PMID:24674022</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4krt" style="background-color:#fffaf0;"></div>

==See Also==
*[[Lysin 3D structures|Lysin 3D structures]]
== References ==
<references/>
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</StructureSection>
[[Category: Clostridium phage phiSM101]]
[[Category: Large Structures]]
[[Category: Kamitori S]]
[[Category: Yoshida H]]