View source for 6ssc


==N-acetylmuramoyl-L-alanine amidase LysC from Clostridium intestinale URNW==
<StructureSection load='6ssc' size='340' side='right'caption='[[6ssc]], [[Resolution|resolution]] 1.21&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6ssc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridium_intestinale Clostridium intestinale]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6SSC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6SSC 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]] 1.21&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <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=6ssc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ssc OCA], [https://pdbe.org/6ssc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ssc RCSB], [https://www.ebi.ac.uk/pdbsum/6ssc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ssc ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/U2NM08_9CLOT U2NM08_9CLOT] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Peptidoglycan hydrolytic enzymes are considered to be a promising alternative to conventional antibiotics in combating bacterial infections. To identify novel hydrolytic enzymes, we performed a database search with the sequences of two thermostable endolysins with high bactericidal activity, studied earlier in our laboratory. Both these enzymes originate from Thermus scotoductus bacteriophages MAT2119 and vB_Tsc2631. A lytic enzyme LysC from Clostridium intestinale URNW was found to have the highest amino acid sequence similarity to the bacteriophage proteins and was chosen for further analysis. The recombinant enzyme showed strong activity against its host bacteria C. intestinale, as well as against C. sporogenes, Bacillus cereus, Micrococcus luteus, and Staphylococcus aureus, on average causing a 5.12 +/- 0.14 log reduction of viable S. aureus ATCC 25923 cells in a bactericidal assay. Crystallographic studies of the protein showed that the catalytic site of LysC contained a zinc atom coordinated by amino acid residues His(50), His(147), and Cys(155), a feature characteristic for type 2 amidases. Surprisingly, neither of these residues, nor any other of the four conserved residues in the vicinity of the active site, His(51), Thr(52), Tyr(76), and Thr(153), were essential to maintain the antibacterial activity of LysC. Therefore, our attention was attracted to the intrinsically disordered and highly positively charged N-terminal region of the enzyme. Potential antibacterial activity of this part of the sequence, predicted by the Antimicrobial Sequence Scanning System, AMPA, was confirmed in our experimental studies; the truncated version of LysC (LysCDelta2-23) completely lacked antibacterial activity. Moreover, a synthetic peptide, which we termed Intestinalin, with a sequence identical to the first thirty amino acids of LysC, displayed substantial anti-staphylococcal activity with IC50 of 6 mug/mL (1.5 muM). This peptide was shown to have alpha-helical conformation in solution in the presence of detergents which is a common feature of amphipathic alpha-helical antimicrobial peptides.

Molecular Characterization of a Novel Lytic Enzyme LysC from Clostridium intestinale URNW and Its Antibacterial Activity Mediated by Positively Charged N-Terminal Extension.,Plotka M, Szadkowska M, Hakansson M, Kovacic R, Al-Karadaghi S, Walse B, Werbowy O, Kaczorowska AK, Kaczorowski T Int J Mol Sci. 2020 Jul 11;21(14). pii: ijms21144894. doi: 10.3390/ijms21144894. PMID:32664473<ref>PMID:32664473</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6ssc" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Clostridium intestinale]]
[[Category: Large Structures]]
[[Category: Al-Karadaghi S]]
[[Category: Hakansson M]]
[[Category: Kaczorowska AK]]
[[Category: Kaczorowski T]]
[[Category: Kovacic R]]
[[Category: Plotka M]]