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Structure and dynamics of the ASB9 CUL-RING E3 Ligase.

Nat Commun. 2020 Jun 08;11(1):2866
Ryan J Lumpkin 1 , Richard W Baker 2 , Andres E Leschziner 3 , Elizabeth A Komives 4
Ryan J Lumpkin 1 , Richard W Baker 2 , Andres E Leschziner 3 , Elizabeth A Komives 4

[No authors listed]

Author information
  • 1 Department of Chemistry and Biochemistry, University of California, San Diego, 9500 Gilman Drive, La Jolla, CA, 92092-0378, USA.
  • 2 Lineberger Comprehensive Cancer Center, University of North Carolina, Chapel Hill, Chapel Hill, NC, USA.
  • 3 Section of Molecular Biology, Division of Biological Sciences, University of California, San Diego, La Jolla, CA, 92093, USA.
  • 4 Department of Chemistry and Biochemistry, University of California, San Diego, 9500 Gilman Drive, La Jolla, CA, 92092-0378, USA. ekomives@ucsd.edu.

摘要

The Cullin 5 (CUL5) Ring E3 ligase uses adaptors Elongins B and C (ELOB/C) to bind different SOCS-box-containing substrate receptors, determining the substrate specificity of the ligase. The 18-member ankyrin and SOCS box (ASB) family is the largest substrate receptor family. Here we report cryo-EM data for the substrate, creatine kinase (CKB) bound to ASB9-ELOB/C, and for full-length CUL5 bound to the RING protein, RBX2, which binds various E2s. To date, no full structures are available either for a substrate-bound ASB nor for CUL5. Hydrogen-deuterium exchange (HDX-MS) mapped onto a full structural model of the ligase revealed long-range allostery extending from the substrate through CUL5. We propose a revised allosteric mechanism for how CUL-E3 ligases function. ASB9 and CUL5 behave as rigid rods, connected through a hinge provided by ELOB/C transmitting long-range allosteric crosstalk from the substrate through CUL5 to the RBX2 flexible linker.

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