Additional file 4 of Discovery, structural characteristics and evolutionary analyses of functional domains in Acinetobacter baumannii phage tail fiber/spike proteins

Supplementary Material 4: Fig. S4. Structural modeling of β-Helix topology in tail fiber/spike proteins not annotated by InterPro as containing PLD. This figure presents the structural modeling of β-helix topology in tail fiber/spike proteins previously reported to have depolymerase activity but not annotated by InterPro (AbTJ 3714, AbP2 2740, vB_AbaM_IME285 16841). The structures reveal short α-helices and β-strands, both highlighted in red, seamlessly integrated into the β-helix units without disrupting their overall topology or functionality.

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Publication Details

Journal
Figshare
Published
2025-01-01
DOI
https://doi.org/10.6084/m9.figshare.28406234
Primary Topic
Bacteriophages and microbial interactions
Type
article
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article

Additional file 4 of Discovery, structural characteristics and evolutionary analyses of functional domains in Acinetobacter baumannii phage tail fiber/spike proteins

Figshare
Bacteriophages and microbial interactions
article

Additional file 4 of Discovery, structural characteristics and evolutionary analyses of functional domains in Acinetobacter baumannii phage tail fiber/spike proteins

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Abstract

Supplementary Material 4: Fig. S4. Structural modeling of β-Helix topology in tail fiber/spike proteins not annotated by InterPro as containing PLD. This figure presents the structural modeling of β-helix topology in tail fiber/spike proteins previously reported to have depolymerase activity but not annotated by InterPro (AbTJ 3714, AbP2 2740, vB_AbaM_IME285 16841). The structures reveal short α-helices and β-strands, both highlighted in red, seamlessly integrated into the β-helix units without disrupting their overall topology or functionality.

Figshare
Guangdong University of Technology (CN), Xiangnan University (CN)
Life below water
Openalex Percentile: Top 50%
Bacteriophages and microbial interactions
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