5nm7

Crystal structure of Burkholderia AP3 phage endolysin

spinqualitylabelsall models 5nm7, resolution 1.72Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5nm7 is a 2 chain structure with sequence from Burkholderia. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.72Å Ligands: GLY, PGE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A1S5NV50_9CAUD Publication Abstract from PubMed Endolysins are peptidoglycan-degrading enzymes utilized by bacteriophages to release the progeny from bacterial cells. The lytic properties of phage endolysins make them potential antibacterial agents for medical and industrial applications. Here, we present a comprehensive characterization of phage AP3 modular endolysin (AP3gp15) containing cell wall binding domain and an enzymatic domain (DUF3380 by BLASTP), both widespread and conservative. Our structural analysis demonstrates the low similarity of an enzymatic domain to known lysozymes and an unusual catalytic centre characterized by only a single glutamic acid residue and no aspartic acid. Thus, our findings suggest distinguishing a novel class of muralytic enzymes having the activity and catalytic centre organization of DUF3380. The lack of amino acid sequence homology between AP3gp15 and other known muralytic enzymes may reflect the evolutionary convergence of analogous glycosidases. Moreover, the broad antibacterial spectrum, lack of cytotoxic effect on human cells and the stability characteristics of AP3 endolysin advocate for its future application development. Modular endolysin of Burkholderia AP3 phage has the largest lysozyme-like catalytic subunit discovered to date and no catalytic aspartate residue.,Maciejewska B, Zrubek K, Espaillat A, Wisniewska M, Rembacz KP, Cava F, Dubin G, Drulis-Kawa Z Sci Rep. 2017 Nov 6;7(1):14501. doi: 10.1038/s41598-017-14797-9. PMID:29109551 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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