Fig. 2: Structures of ΦKZ’s MCP monomers. | Nature Communications

Fig. 2: Structures of ΦKZ’s MCP monomers.

From: Capsid structure of bacteriophage ΦKZ provides insights into assembly and stabilization of jumbo phages

Fig. 2

a Ribbon diagrams of the representative MCP subunit from the hexameric capsomer 3 (subunit r, left) and the subunit from the pentameric capsomer (subunit A, right). The N-terminal arm (blue, residues 164–204), I-domain linkers (cyan, residues 205–247 and residues 473–484), I domain (green, residues 248–472), P domain (yellow, residues 485–539 and 680–717), A domain (orange, residues 540–679 and 718–727) and C-terminal arm (magenta, residues 728–747) are labeled. b Structural alignment of the MCP subunit r and subunit A based on their A domains shows that the MCP from the pentameric capsomer (subunit A) adopted a more curved conformation. Additional structural alignment of all the 27 MCP subunits within one icosahedral asymmetric unit is shown in Supplementary Fig. 5a. c Structural alignments of ΦKZ’s MCP subunits and ΦKp24’s MCP subunits (PDB: 8BFL, 8BFP) (left: alignment of subunits y from hexameric capsomer 5, right: alignment of subunits A from the pentameric capsomer). NTA, N-terminal arm. CTA, C-terminal arm.

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