8p8e: Difference between revisions
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New page: '''Unreleased structure''' The entry 8p8e is ON HOLD Authors: van Raaij, M.J., Sanz-Gaitero, M. Description: Crystal structure of endolysin gp46 from Pseudomonas aeruginosa bacteriopha... |
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==Crystal structure of endolysin gp46 from Pseudomonas aeruginosa bacteriophage vB_PaeM_KTN6== | |||
<StructureSection load='8p8e' size='340' side='right'caption='[[8p8e]], [[Resolution|resolution]] 1.39Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8p8e]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacteriophage_sp. Bacteriophage sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8P8E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8P8E 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]] 1.391Å</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=8p8e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8p8e OCA], [https://pdbe.org/8p8e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8p8e RCSB], [https://www.ebi.ac.uk/pdbsum/8p8e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8p8e ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A9E7MJ36_9CAUD A0A9E7MJ36_9CAUD] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
BACKGROUND: Endolysins are phage-encoded lytic enzymes that degrade bacterial peptidoglycan at the end of phage lytic cycles to release new phage particles. These enzymes are being explored as an alternative to small-molecule antibiotics. METHODS: The crystal structure of KTN6 Gp46 was determined and compared with a ColabFold model. Cleavage specificity was examined using a peptidoglycan digest and reversed-phase high-performance liquid chromatography coupled to mass spectrometry (HPLC/MS). RESULTS: The structure of KTN6 Gp46 could be determined at 1.4 A resolution, and key differences in loops of the putative peptidoglycan binding domain were identified in comparison with its closest known homologue, the endolysin of phage SPN1S. Reversed-phase HPLC/MS analysis of the reaction products following peptidoglycan digestion confirmed the muramidase activity of Gp46, consistent with structural predictions. CONCLUSION: These insights into the structure and function of endolysins further expand the toolbox for endolysin engineering and explore their potential in enzyme-based antibacterial design strategies. | |||
Structural and Biochemical Characterization of a New Phage-Encoded Muramidase, KTN6 Gp46.,Sanz-Gaitero M, De Maesschalck V, Patel A, Longin H, Van Noort V, Rodriguez-Rubio L, van Ryne M, Danis-Wlodarczyk K, Drulis-Kawa Z, Mesnage S, van Raaij M, Lavigne R Phage (New Rochelle). 2024 Jun 21;5(2):53-62. doi: 10.1089/phage.2023.0040. , eCollection 2024 Jun. PMID:39119210<ref>PMID:39119210</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: Sanz-Gaitero | <div class="pdbe-citations 8p8e" style="background-color:#fffaf0;"></div> | ||
[[Category: Van Raaij | == References == | ||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Bacteriophage sp]] | |||
[[Category: Large Structures]] | |||
[[Category: Sanz-Gaitero M]] | |||
[[Category: Van Raaij MJ]] | |||
Latest revision as of 13:14, 21 August 2024
Crystal structure of endolysin gp46 from Pseudomonas aeruginosa bacteriophage vB_PaeM_KTN6
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