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Title: High-resolution structure of podovirus tail adaptor suggests repositioning of an octad motif that mediates the sequential tail assembly

Journal Article · · Proceedings of the National Academy of Sciences of the United States of America

The sophisticated tail structures of DNA bacteriophages play essential roles in life cycles. Podoviruses P22 and Sf6 have short tails consisting of multiple proteins, among which is a tail adaptor protein that connects the portal protein to the other tail proteins. Assembly of the tail has been shown to occur in a sequential manner to ensure proper molecular interactions, but the underlying mechanism remains to be understood. Here, we report the high-resolution structure of the tail adaptor protein gp7 from phage Sf6. The structure exhibits distinct distribution of opposite charges on two sides of the molecule. A gp7 dodecameric ring model shows an entirely negatively charged surface, suggesting that the assembly of the dodecamer occurs through head-to-tail interactions of the bipolar monomers. The N-terminal helix-loop structure undergoes rearrangement compared with that of the P22 homolog complexed with the portal, which is achieved by repositioning of two consecutive repeats of a conserved octad sequence motif. We propose that the conformation of the N-terminal helix-loop observed in the Sf6-gp7 and P22 portal:gp4 complex represents the pre- and postassembly state, respectively. Such motif repositioning may serve as a conformational switch that creates the docking site for the tail nozzle only after the assembly of adaptor protein to the portal. In addition, the C-terminal portion of gp7 shows conformational flexibility, indicating an induced fit on binding to the portal. Furthermore, these results provide insight into the mechanistic role of the adaptor protein in mediating the sequential assembly of the phage tail.

Research Organization:
Argonne National Laboratory (ANL), Argonne, IL (United States)
Sponsoring Organization:
National Inst. of General Medical Sciences of the National Inst. of Health
Grant/Contract Number:
R01GM090010; P30 GM103326
OSTI ID:
1424789
Journal Information:
Proceedings of the National Academy of Sciences of the United States of America, Vol. 115, Issue 2; ISSN 0027-8424
Publisher:
National Academy of SciencesCopyright Statement
Country of Publication:
United States
Language:
ENGLISH
Citation Metrics:
Cited by: 7 works
Citation information provided by
Web of Science

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Cited By (2)

Complete genome analysis of the novel Enterococcus faecalis phage vB_EfaS_AL3 journal July 2019
Structures of T7 bacteriophage portal and tail suggest a viral DNA retention and ejection mechanism journal August 2019

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