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Cdc123 protein structure reveals how it aids eukaryotic initiation factor 2 (eIF2) assembly, crucial for protein synthesis. ATP binding is vital for Cdc123 function in eIF2 assembly, impacting conditions like MEHMO syndrome.

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Area of Science:

  • Molecular Biology
  • Structural Biology
  • Biochemistry

Background:

  • Eukaryotic initiation factor 2 (eIF2) is essential for protein synthesis and its regulation.
  • Cdc123 protein facilitates eIF2 assembly, and mutations in it are linked to MEHMO syndrome, an intellectual disability.

Purpose of the Study:

  • To elucidate the structural basis of human Cdc123 (Hs-Cdc123) interaction with eIF2γ.
  • To understand the role of ATP in Hs-Cdc123 mediated eIF2 assembly.

Main Methods:

  • Crystallography to determine the structure of Hs-Cdc123 bound to Hs-eIF2γD3.
  • Thermal shift assay to assess ATP and ADP binding.
  • Yeast cell viability, western blot, and two-hybrid assays to evaluate protein function.

Main Results:

  • The crystal structure reveals Hs-eIF2γD3 binding to domain 1 of Hs-Cdc123, with the C-terminal region linking ATP and eIF2γ binding sites.
  • ATP binds tightly to Hs-Cdc123, while ADP has low affinity.
  • ATP is essential for Hs-Cdc123 function in eIF2 assembly.

Conclusions:

  • A structural model for Hs-Cdc123 action in eIF2 assembly is proposed.
  • Understanding Cdc123 function provides insights into protein synthesis regulation and MEHMO syndrome.