Structural and functional characterization of the deep-sea thermophilic bacteriophage GVE2 tailspike protein

The genome of the thermophilic bacteriophage GVE2 encodes a putative tailspike protein (GVE2 TSP). Here we report the crystal structure of the truncated GVE2 TSP at 2.0-Å resolution lacking 204 amino acid residues at its N-terminus (ΔnGVE2 TSP), possessing a “vase” outline similar to other TSP'...

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Bibliographic Details
Published in:International journal of biological macromolecules 2020-12, Vol.164, p.4415-4422
Main Authors: Zhang, Likui, Yan, Yuhua, Gan, Qi, She, Zhun, Zhu, Keli, Wang, Jinhui, Gao, Zengqiang, Dong, Yuhui, Gong, Yong
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Aquatic Organisms
Bacteriophages - classification
Bacteriophages - genetics
Bacteriophages - physiology
Cloning, Molecular
Crystal structure
Enzyme Activation
Gene Expression
Models, Molecular
Phylogeny
Protein Conformation
Protein Domains
Recombinant Proteins
Structure-Activity Relationship
Tailspike protein
Thermophilic bacteriophage
Viral Tail Proteins - chemistry
Viral Tail Proteins - genetics
Viral Tail Proteins - metabolism
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Summary:The genome of the thermophilic bacteriophage GVE2 encodes a putative tailspike protein (GVE2 TSP). Here we report the crystal structure of the truncated GVE2 TSP at 2.0-Å resolution lacking 204 amino acid residues at its N-terminus (ΔnGVE2 TSP), possessing a “vase” outline similar to other TSP's structures. However, ΔnGVE2 TSP displays structural characteristics distinct from other TSPs. Despite lacking 204 amino acid residues, the head domain forms an asymmetric trimer compared to symmetric in other TSPs, suggesting that its long N-terminus may be unique to the long-tailed bacteriophages. Furthermore, the α-helix of the neck is 5–7 amino acids longer than that of other TSPs. The most striking feature is that its binding domain consists of a β-helix with 10 turns, whereas other TSPs have 13 turns, even including the phage Sf6 TSP, which is the closest homologue of GVE2 TSP. The C-terminal structure is also quite different with those of other TSPs. Furthermore, we observed that ΔnGVE2 TSP can slow down growth of its host, demonstrating that this TSP is essential for the phage GVE2 to infect its host. Overall, the structural characteristics suggest that GVE2 TSP may be more primitive than other phage TSPs.
ISSN:0141-8130
1879-0003
DOI:10.1016/j.ijbiomac.2020.09.053