Structure of T5-Like Phage dUTPase from Vibrio Phage Phi3

The first crystal structure of dUTPase from the bacteriophage Vibrio phage phi3 was determined at 1.95 Å resolution. This protein has a homotrimeric quaternary structure characteristic of this type of dUTPases and contains a short loop in the N-terminal region of the polypeptide chain, which is specific for Т5-like bacteriophage dUTPases. It was demonstrated that, despite a low amino acid sequence homology between phage (Т5 and phi3) dUTPases, phi3 dUTPase can effectively replace phage Т5 dUTPase during the lytic cycle.

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Journal
Crystallography Reports
Published
2024-12-01
DOI
https://doi.org/10.1134/s1063774524602041
Primary Topic
Bacteriophages and microbial interactions
Type
article
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article

Structure of T5-Like Phage dUTPase from Vibrio Phage Phi3

Azat Gabdulkhakov, Ulyana Dzhus, Georgii Selikhanov, Anatoly Glukhov et al.
Crystallography Reports
Bacteriophages and microbial interactions
article

Structure of T5-Like Phage dUTPase from Vibrio Phage Phi3

Azat Gabdulkhakov, Ulyana Dzhus, Georgii Selikhanov, Anatoly Glukhov, Ilya Kolyadenko
article en

Abstract

The first crystal structure of dUTPase from the bacteriophage Vibrio phage phi3 was determined at 1.95 Å resolution. This protein has a homotrimeric quaternary structure characteristic of this type of dUTPases and contains a short loop in the N-terminal region of the polypeptide chain, which is specific for Т5-like bacteriophage dUTPases. It was demonstrated that, despite a low amino acid sequence homology between phage (Т5 and phi3) dUTPases, phi3 dUTPase can effectively replace phage Т5 dUTPase during the lytic cycle.

Crystallography ReportsVol. 69(7)
ITMO University (RU), Institute of Protein Research (RU)
Zero hunger
Openalex Percentile: Top 74%
Bacteriophages and microbial interactions
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