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Structure paper

TitleMultifaceted N-Degron Recognition and Ubiquitylation by GID/CTLH E3 Ligases.
Journal, issue, pagesJ. Mol. Biol., Vol. 434, Page 167347-167347, Year 2022
Publish dateNov 2, 2021 (structure data deposition date)
AuthorsChrustowicz, J. / Sherpa, D. / Teyra, J. / Loke, M.S. / Popowicz, G.M. / Basquin, J. / Sattler, M. / Prabu, J.R. / Sidhu, S.S. / Schulman, B.A.
External linksJ. Mol. Biol. / PubMed:34767800
MethodsX-ray diffraction
Resolution2.22 - 3.16 Å
Structure data

PDB-7q4y:
human Gid4 bound to a Gly/N-peptide
Method: X-RAY DIFFRACTION / Resolution: 3.08 Å

PDB-7q50:
human Gid4 bound to a Phe/N-peptide
Method: X-RAY DIFFRACTION / Resolution: 3.16 Å

PDB-7q51:
yeast Gid10 bound to a Phe/N-peptide
Method: X-RAY DIFFRACTION / Resolution: 2.22 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-CL:
Unknown entry

Source
  • homo sapiens (human)
  • saccharomyces cerevisiae s288c (yeast)
  • saccharomyces cerevisiae (brewer's yeast)
KeywordsLIGASE / GID / CTLH / ubiquitin / E3 ligase / metabolism

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