7CHU

Geobacillus virus E2 - ORF18

Summary for 7CHU

• Entry DOI: 10.2210/pdb7chu/pdb
• Descriptor: Putative pectin lyase (2 entities in total)
• Functional Keywords: tailspike protein, thermophilic bacteriophage, cell invasion
• Biological source: Geobacillus virus E2
• Total number of polymer chains: 3
• Total formula weight: 170087.98

Authors

Gong, Y. (deposition date: 2020-07-06, release date: 2021-04-14, Last modification date: 2024-03-27)

Primary citation

Zhang, L.,Yan, Y.,Gan, Q.,She, Z.,Zhu, K.,Wang, J.,Gao, Z.,Dong, Y.,Gong, Y.
Structural and functional characterization of the deep-sea thermophilic bacteriophage GVE2 tailspike protein.
Int.J.Biol.Macromol., 164:4415-4422, 2020

PubMed Abstract: 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.

PubMed: 32926904
DOI: 10.1016/j.ijbiomac.2020.09.053

Experimental method

X-RAY DIFFRACTION (2.008 Å)