NMR structure of protein yqbG from <i>Bacillus subtilis</i> reveals a novel α‐helical protein fold

Liu, Gaohua; Shen, Yang; Xiao, Rong; Acton, T.B.; Chung, Li; Joachimiak, Andrzej; Montelione, Gaetano T.; Szyperski, Thomas

doi:10.1002/prot.20666

Cited by 3 publications

(4 citation statements)

References 20 publications

(21 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…3 c and 5a, b ). Interestingly, in the non-assembled monomer of the gp15 homologue YqbG 34 helix α0 adopts a position, stabilized by intrachain bonds, that is close to the orientation found in the gp15 connector state (Supplementary Fig. 6b ).…”

Section: Discussionmentioning

confidence: 76%

See 1 more Smart Citation

CryoEM structure and assembly mechanism of a bacterial virus genome gatekeeper

et al. 2022

View full text Add to dashboard Cite

Numerous viruses package their dsDNA genome into preformed capsids through a portal gatekeeper that is subsequently closed. We report the structure of the DNA gatekeeper complex of bacteriophage SPP1 (gp612gp1512gp166) in the post-DNA packaging state at 2.7 Å resolution obtained by single particle cryo-electron microscopy. Comparison of the native SPP1 complex with assembly-naïve structures of individual components uncovered the complex program of conformational changes leading to its assembly. After DNA packaging, gp15 binds via its C-terminus to the gp6 oligomer positioning gp15 subunits for oligomerization. Gp15 refolds its inner loops creating an intersubunit β-barrel that establishes different types of contacts with six gp16 subunits. Gp16 binding and oligomerization is accompanied by folding of helices that close the portal channel to keep the viral genome inside the capsid. This mechanism of assembly has broad functional and evolutionary implications for viruses of the prokaryotic tailed viruses-herpesviruses lineage.

show abstract

Section: Discussionmentioning

confidence: 76%

“…The NMR structures of gp15 and YqbG monomers 19 , 34 both show highly mobile loops α2-α3 (Supplementary Fig. 6b ).…”

Section: Discussionmentioning

confidence: 99%

CryoEM structure and assembly mechanism of a bacterial virus genome gatekeeper

et al. 2022

View full text Add to dashboard Cite

show abstract

“…18 Interestingly, the structure of YqbG is considerably closer to that of gp6 than is gp15 with 71 residues overlaying with an RMSD of only 1.8 Å (Fig. 8a).…”

Section: Resultsmentioning

confidence: 91%

The Crystal Structure of Bacteriophage HK97 gp6: Defining a Large Family of Head–Tail Connector Proteins

Cardarelli

Lam

Tuite

et al. 2010

Journal of Molecular Biology

View full text Add to dashboard Cite

“…Despite low sequence homology, this protein fold is common in tail adaptor proteins of podoviruses, siphoviruses, and probably myoviruses as well. Structural superimposition shows a (27) (Fig. S1B).…”

Section: Resultsmentioning

confidence: 99%

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

Liang

Zhao

et al. 2017

Proc. Natl. Acad. Sci. U.S.A.

View full text Add to dashboard Cite

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. These results provide insight into the mechanistic role of the adaptor protein in mediating the sequential assembly of the phage tail.

show abstract

NMR structure of protein yqbG from Bacillus subtilis reveals a novel α‐helical protein fold

Cited by 3 publications

References 20 publications

CryoEM structure and assembly mechanism of a bacterial virus genome gatekeeper

CryoEM structure and assembly mechanism of a bacterial virus genome gatekeeper

The Crystal Structure of Bacteriophage HK97 gp6: Defining a Large Family of Head–Tail Connector Proteins

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

Contact Info

Product

Resources

About