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TitleDirect Visualization of a 26 kDa Protein by Cryo-Electron Microscopy Aided by a Small Scaffold Protein.
Journal, issue, pagesBiochemistry, Vol. 60, Issue 14, Page 1075-1079, Year 2021
Publish dateApr 13, 2021
AuthorsYi-Hsiang Chiu / Kuang-Ting Ko / Tzu-Jing Yang / Kuen-Phon Wu / Meng-Ru Ho / Piotr Draczkowski / Shang-Te Danny Hsu /
PubMed AbstractCryo-electron microscopy (cryo-EM)-based structure determination of small proteins is hindered by the technical challenges associated with low signal-to-noise ratios of their particle images in ...Cryo-electron microscopy (cryo-EM)-based structure determination of small proteins is hindered by the technical challenges associated with low signal-to-noise ratios of their particle images in intrinsically noisy micrographs. One solution is to attach the target protein to a large protein scaffold to increase its apparent size and, therefore, image contrast. Here we report a novel scaffold design based on a trimeric helical protein, ornithine transcarbamylase (OTC), fused to human ubiquitin. As a proof of principle, we demonstrated the ability to resolve a cryo-EM map of a 26 kDa human ubiquitin C-terminal hydrolase (UCHL1) attached to the C-terminus of ubiquitin as part of the trimeric assembly. The results revealed conformational changes in UCHL1 upon binding to ubiquitin, namely, a significant displacement of α-helix 2, which was also observed by X-ray crystallography. Our findings demonstrated the potential of the trimeric OTC scaffold design for studying a large number of ubiquitin interacting proteins by cryo-EM.
External linksBiochemistry / PubMed:33719392
MethodsEM (single particle)
Resolution4.1 Å
Structure data

EMDB-30634:
Cryo-EM structure of Ornithine transcarbamylase fused with Ubiquitin in complex with Ubiquitin-carboxy-hydrolase-L1 crosslinked with BS3
Method: EM (single particle) / Resolution: 4.1 Å

Source
  • Escherichia coli (E. coli)

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