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TitleAffinity Capture of p97 with Small-Molecule Ligand Bait Reveals a 3.6 Å Double-Hexamer Cryoelectron Microscopy Structure.
Journal, issue, pagesACS Nano, Vol. 15, Issue 5, Page 8376-8385, Year 2021
Publish dateMay 25, 2021
AuthorsMd Rejaul Hoq / Frank S Vago / Kunpeng Li / Marina Kovaliov / Robert J Nicholas / Donna M Huryn / Peter Wipf / Wen Jiang / David H Thompson /
PubMed AbstractRecent progress in the development of affinity grids for cryoelectron microscopy (cryo-EM) typically employs genetic engineering of the protein sample such as histidine or Spy tagging, immobilized ...Recent progress in the development of affinity grids for cryoelectron microscopy (cryo-EM) typically employs genetic engineering of the protein sample such as histidine or Spy tagging, immobilized antibody capture, or nonselective immobilization via electrostatic interactions or Schiff base formation. We report a powerful and flexible method for the affinity capture of target proteins for cryo-EM analysis that utilizes small-molecule ligands as bait for concentrating human target proteins directly onto the grid surface for single-particle reconstruction. This approach is demonstrated for human p97, captured using two different small-molecule high-affinity ligands of this AAA+ ATPase. Four electron density maps are revealed, each representing a p97 conformational state captured from solution, including a double-hexamer structure resolved to 3.6 Å. These results demonstrate that the noncovalent capture of protein targets on EM grids modified with high-affinity ligands can enable the structure elucidation of multiple configurational states of the target and potentially inform structure-based drug design campaigns.
External linksACS Nano / PubMed:33900731
MethodsEM (single particle)
Resolution3.57 - 4.22 Å
Structure data

EMDB-23927:
Cryo-EM structure of affinity captured human p97 hexamer
Method: EM (single particle) / Resolution: 4.22 Å

EMDB-23928:
Cryo-EM structure of affinity captured human p97 double-hexamer
Method: EM (single particle) / Resolution: 3.57 Å

Source
  • Homo sapiens (human)

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