Biochemical and structural characterization of a tail-spike protein with depolymerase activity identified in a marine podovirus

Sirigu, S.; Roret, T.; Mocaër, P.-Y.; Larocque, R.; Jouanneau, D.; Legrand, P.; Baudoux, A.-C.; Czjzek, M.

doi:10.1107/S2059798326005425

Acta Crystallographica Section D
Acta Crystallographica
Section D STRUCTURAL BIOLOGY

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Figure 5
Ribbon representation of the structural organization of D4 as observed in the crystal structure of the isolated domain. (a) Side view and (b) top view of the trimeric organization of D4. (c) Ribbon representation of the bent structure of Dpo31 that was fitted into the cryo-EM electron density (d'Acapito et al., 2023

). Three disordered regions between D1 and D2, within D2 and between D2 and D3 are responsible for bending.

STRUCTURAL
BIOLOGY

ISSN: 2059-7983

Volume 82| Part 7| July 2026| Pages 785-799

https://doi.org/10.1107/S2059798326005425

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