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TitleThe Lord of the Rings: Cysteine bonds crosslink the tail of siphovirus.
Journal, issue, pagesProtein Sci, Vol. 35, Issue 10, Page e70784, Year 2026
Publish dateSep 15, 2026
AuthorsSimona Povilonienė / Giedrius Sasnauskas / Giedrė Tamulaitienė / Greta Labutytė / Martynas Talaikis / Algirdas Mikšys / Aurelija Zajančkauskaitė / Lidija Truncaitė / Rolandas Meškys / Vida Časaitė
PubMed AbstractLong, non-contractile tails composed of helical hexameric protein repeats that assemble into continuous tubular structures characterize siphoviruses. The siphovirus tail tube protein gp39 contains ...Long, non-contractile tails composed of helical hexameric protein repeats that assemble into continuous tubular structures characterize siphoviruses. The siphovirus tail tube protein gp39 contains two cysteine residues per monomer. Cryo-electron microscopy revealed that these cysteines are oriented toward the interface between the rings, which facilitates the formation of inter-ring disulfide bonds. Phylogenetic analysis revealed that in the phage tail tube protein-3 (PF08813) family, only a single branch, representing approximately 14% of its members, contains disulfide bonds within the tubular structure, indicating a clear evolutionary adaptation to stabilize the structure. Structural characterization of gp39 alongside its homolog gp13, which naturally lacks disulfide crosslinks, provided insight into this stabilization strategy. Both gp39 and gp13 can self-assemble into tubular structures independently of disulfide bond formation. When cysteine residues were inserted into gp13 at the same positions as in gp39, disulfide bonds were formed, as confirmed by Raman spectroscopy. Differential scanning fluorimetry further demonstrated that variants containing disulfide bonds exhibit enhanced thermal stability. These results reveal the evolutionary and structural basis by which disulfide bonds ensure the stability of phage tail structures and establish the fundamental principles for the design of robust, thermally stable protein nanotubes.
External linksProtein Sci / PubMed:42742064 / PubMed Central
MethodsEM (helical sym.) / EM (single particle)
Resolution2.9 - 4.89 Å
Structure data

56097

9to0

EMDB-56097, PDB-9to0:
gp13 protein from vB_PagS_MED16 bacteriophage
Method: EM (helical sym.) / Resolution: 2.9 Å

56098

9toi

EMDB-56098, PDB-9toi:
gp39 protein from Escherichia phage vB_EcoS_NBD2
Method: EM (single particle) / Resolution: 3.3 Å

EMDB-56099: gp39 protein from Escherichia phage vB_EcoS_NBD2, unbent tubule, helix refine consensus map
Method: EM (helical sym.) / Resolution: 4.89 Å

EMDB-56100: gp39 protein from Escherichia phage vB_EcoS_NBD2, unbent tubule, focused map 1
Method: EM (single particle) / Resolution: 3.11 Å

EMDB-56101: gp39 protein from Escherichia phage vB_EcoS_NBD2, unbent tubule, focused map 2
Method: EM (single particle) / Resolution: 3.26 Å

56103

9toz

EMDB-56103, PDB-9toz:
gp39 protein from Escherichia phage vB_EcoS_NBD2, unbent tubule
Method: EM (single particle) / Resolution: 3.1 Å

Source
  • pantoea phage vb_pags_med16 (virus)
  • escherichia phage vb_ecos_nbd2 (virus)
KeywordsVIRAL PROTEIN / vB_PagS_MED16 bacteriophage / bacteriophage tail / vB_EcoS_NBD2 bacteriophage

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