Fig. 4: Structure of MOS-bound OsISA1-ISA2 heterocomplex. | Nature Communications

Fig. 4: Structure of MOS-bound OsISA1-ISA2 heterocomplex.

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

Fig. 4

a Cryo-EM density map and surface representation of MOS-bound OsISA1-ISA2 heterocomplex. OsISA1 protomers are colored in yellow green and royal blue, OsISA2 in violet, and MOS in orange. b Structural superposition of MOS-free and MOS-bound OsISA1-ISA2 heterocomplex. MOS-free OsISA1-ISA2 is colored in light gray. c Structural superposition of MOS-bound OsISA1-ISA2 heterocomplex with MOS-bound CrISA1 dimer. MOS-bound CrISA1 dimer is colored in cyan. d The interaction networks of MOS in the catalytic pocket of OsISA1. The maltoheptaose and the free glucose molecules are labeled. Surrounding residues within 4 Å are shown in sticks. The catalytic triad are shown in green sticks. e, f Maltotriose-binding cleft within OsISA1. g Four glucose molecules are shown in the C-terminal segment of OsISA2. Surrounding residues within 4 Å are shown in sticks.

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