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Fig. 3 | BMC Microbiology

Fig. 3

From: Characterization of a novel lytic phage vB_AbaM_AB4P2 encoding depolymerase and its application in eliminating biofilms formed by Acinetobacter baumannii

Fig. 3

The genomic structure of A. baumannii phage vB_AbaM_AB4P2 and its functional domain responsible for depolymerase activity. (a) Schematic genomic alignment with Salmonella phage IME207, Salmonella phage vB_Se_STGO-35-1, and Escherichia phage C1 generated using EasyFig. The bar in the lower right corner shows the identity percentage for normal and inverted BLAST matches. (b) 3D structural analysis of the tail fiber protein WPJ20733 in phage vB_AbaM_AB4P2. The structure of this protein, predicted using AlphaFold3, is shown in both its monomeric form (left) and trimeric assembly (right). The pectin lyase-like domain (colored in blue) adopts a right-handed parallel β-helix structure, which is crucial for substrate binding and catalytic activity

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BMC Microbiology

ISSN: 1471-2180

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