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. Author manuscript; available in PMC: 2024 Aug 15.

Published in final edited form as: Biochemistry. 2023 Jul 25;62(16):2461–2471. doi: 10.1021/acs.biochem.3c00180

Figure 4. — Conservation between hhYR/hhCF and fused 4OT, a representative asymmetric 4-OT trimer.⁵ (A) Multiple sequence alignment between the α- and β-chains of hhYR/hhCF and one protomer of the representative fused 4OT. Conserved salt bridge partners are highlighted and outlined between the α and β subunits. Highlighted in red is the linker region in fused 4OT Alignment was conducted with Clustal Omega.³⁴ (B) Ribbon diagram of the salt bridge interactions in the ββ interface. Participating subunits are colored in purple (α-subunit) and pink (β-subunit) while chains that are not within the interface are in gray. Salt bridge interactions are shown with dotted blue lines and residues in stick form. Pro1 is shown as a sphere. (C) Salt bridge interactions within the αα interface. (D) Salt bridge interactions within the αβ interface.

Figure 4. — Conservation between hhYR/hhCF and fused 4OT, a representative asymmetric 4-OT trimer.⁵ (A) Multiple sequence alignment between the α- and β-chains of hhYR/hhCF and one protomer of the representative fused 4OT. Conserved salt bridge partners are highlighted and outlined between the α and β subunits. Highlighted in red is the linker region in fused 4OT Alignment was conducted with Clustal Omega.³⁴ (B) Ribbon diagram of the salt bridge interactions in the ββ interface. Participating subunits are colored in purple (α-subunit) and pink (β-subunit) while chains that are not within the interface are in gray. Salt bridge interactions are shown with dotted blue lines and residues in stick form. Pro1 is shown as a sphere. (C) Salt bridge interactions within the αα interface. (D) Salt bridge interactions within the αβ interface.