8app
From Proteopedia
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[8app]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Acinetobacter_phage_AbTZA1 Acinetobacter phage AbTZA1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8APP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8APP FirstGlance]. <br> | <table><tr><td colspan='2'>[[8app]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Acinetobacter_phage_AbTZA1 Acinetobacter phage AbTZA1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8APP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8APP FirstGlance]. <br> | ||
| - | </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></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]] 1.82Å</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></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=8app FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8app OCA], [https://pdbe.org/8app PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8app RCSB], [https://www.ebi.ac.uk/pdbsum/8app PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8app ProSAT]</span></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=8app FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8app OCA], [https://pdbe.org/8app PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8app RCSB], [https://www.ebi.ac.uk/pdbsum/8app PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8app ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/A0A3T0IGR7_9CAUD A0A3T0IGR7_9CAUD] Endolysin with lysozyme activity that degrades host peptidoglycans and participates with the holin and spanin proteins in the sequential events which lead to the programmed host cell lysis releasing the mature viral particles. Once the holin has permeabilized the host cell membrane, the endolysin can reach the periplasm and break down the peptidoglycan layer.[HAMAP-Rule:MF_04110] | [https://www.uniprot.org/uniprot/A0A3T0IGR7_9CAUD A0A3T0IGR7_9CAUD] Endolysin with lysozyme activity that degrades host peptidoglycans and participates with the holin and spanin proteins in the sequential events which lead to the programmed host cell lysis releasing the mature viral particles. Once the holin has permeabilized the host cell membrane, the endolysin can reach the periplasm and break down the peptidoglycan layer.[HAMAP-Rule:MF_04110] | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | The classification of Acinetobacter baumannii by WHO as 'priority 1' antibiotic-resistant pathogen underlines the urgent need for novel antimicrobial agents towards this pathogen. In this work, screening of the A. baumannii phage AbTZA1 genome allowed the identification of a putative endolysin (AbLys1, EC3.2.1.17) that belongs to the glycoside hydrolase family 24 (GH24). The sequence of AbLys1 was cloned, expressed in E. coli and purified. The lytic activity and specificity of AbLys1 were evaluated against a range of Gram-positive and Gram-negative human pathogens. AbLys1 was found to display a high selectivity towards A. baumannii. Kinetic analysis was carried out to characterize the dependence of its lytic activity on pH. The enzyme shows its maximal activity at pH values 7-8. The structure of AbLys1 was determined by X-ray crystallography to 1.82 A resolution. The overall structure revealed two helical domains: a small, antenna-like, N-terminal domain and a larger C-terminal domain with six alpha-helices and a beta-hairpin. Both the antenna-like and beta-hairpin regions contain short sequences (AMseq1 and AMseq2) with predicted antimicrobial activity. Engineering studies revealed a key role of AMseq1 and AMseq2 on the enzyme's lytic activity towards A. baumannii cells but not towards purified peptidoglycan. This suggests that both sequences affect the destabilization of the outer membrane, thus providing access of the catalytic domain to the peptidoglycan. In addition, the deletion of AMseq1 enhanced the enzyme stability, whereas the deletion of AMseq2 diminished it. The results suggest that AbLys1 is a promising new enzybiotic with efficient lytic and antimicrobial activity. | ||
| - | + | ==See Also== | |
| - | + | *[[Lysozyme 3D structures|Lysozyme 3D structures]] | |
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Current revision
AbLys1 endolysin from Acinetobacter baumannii phage AbTZA1
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