Fig. 3: Structure of OsISA1-ISA2 heterocomplex. | Nature Communications

Fig. 3: Structure of OsISA1-ISA2 heterocomplex.

From: Amylopectin branch trimming and biosynthesis elucidated by the rice isoamylase ISA1-ISA2 heterocomplex

Fig. 3

a Cryo-EM density map of the ISA1-ISA2 heterocomplex. ISA1 protomers are colored in slate gray and slate blue, while ISA2 is shown in violet. b Structural model of OsISA1-ISA2 heterocomplex in cartoon representation. Two side orientations are shown. The N and C termini of OsISA2 are indicated. Domain organizations of OsISA2 are shown on top. TP target peptide, NTD N-terminal domain; CBM, Carbohydrate-binding module. AMY, amylase; CT, C-terminal region. c Interactions between ISA1 AMY and ISA2 CBMs. d Interactions between ISA1 AMY and ISA2 AMY. e Interactions between ISA1 CBM and ISA2 AMY. The involved residues are shown in sticks. f, g Key residues validated by co-expression and pull-down assays. The His-tagged OsISA1 and HA-tagged OsISA2 are validated by anti-His and anti-HA, respectively. Asterisks indicate the relative mutants of either OsISA1 or OsISA2. At least three biological replicates were performed.

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