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TitleVisualisation of a flexible modular structure of the ER folding-sensor enzyme UGGT.
Journal, issue, pagesSci Rep, Vol. 7, Issue 1, Page 12142, Year 2017
Publish dateSep 22, 2017
AuthorsTadashi Satoh / Chihong Song / Tong Zhu / Takayasu Toshimori / Kazuyoshi Murata / Yugo Hayashi / Hironari Kamikubo / Takayuki Uchihashi / Koichi Kato /
PubMed AbstractIn the endoplasmic reticulum (ER), a protein quality control system facilitates the efficient folding of newly synthesised proteins. In this system, a series of N-linked glycan intermediates ...In the endoplasmic reticulum (ER), a protein quality control system facilitates the efficient folding of newly synthesised proteins. In this system, a series of N-linked glycan intermediates displayed on the protein surface serve as quality tags. The ER folding-sensor enzyme UDP-glucose:glycoprotein glucosyltransferase (UGGT) acts as a gatekeeper in the ER quality control system by specifically catalysing monoglucosylation onto incompletely folded glycoproteins, thereby enabling them to interact with lectin-chaperone complexes. Here we characterise the dynamic structure of this enzyme. Our crystallographic data demonstrate that the sensor region is composed of four thioredoxin-like domains followed by a β-rich domain, which are arranged into a C-shaped structure with a large central cavity, while the C-terminal catalytic domain undergoes a ligand-dependent conformational alteration. Furthermore, small-angle X-ray scattering, cryo-electron microscopy and high-speed atomic force microscopy have demonstrated that UGGT has a flexible modular structure in which the smaller catalytic domain is tethered to the larger folding-sensor region with variable spatial arrangements. These findings provide structural insights into the working mechanism whereby UGGT operates as a folding-sensor against a variety of glycoprotein substrates through its flexible modular structure possessing extended hydrophobic surfaces for the recognition of unfolded substrates.
External linksSci Rep / PubMed:28939828 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution1.35 - 22.9 Å
Structure data

EMDB-30386:
Negative-stain EM 3D reconstruction of UGGT with the Fab of monoclonal antibody directed against the Trx4 domain.
Method: EM (single particle) / Resolution: 22.9 Å

PDB-5h18:
Crystal structure of catalytic domain of UGGT (UDP-glucose-bound form) from Thermomyces dupontii
Method: X-RAY DIFFRACTION / Resolution: 1.4 Å

PDB-5y7f:
Crystal structure of catalytic domain of UGGT (UDP-bound form) from Thermomyces dupontii
Method: X-RAY DIFFRACTION / Resolution: 1.35 Å

PDB-5y7o:
Crystal structure of folding sensor region of UGGT from Thermomyces dupontii
Method: X-RAY DIFFRACTION / Resolution: 3.1 Å

Chemicals

ChemComp-UPG:
URIDINE-5'-DIPHOSPHATE-GLUCOSE / Uridine diphosphate glucose

ChemComp-CA:
Unknown entry

ChemComp-GOL:
GLYCEROL / Glycerol

ChemComp-HOH:
WATER / Water

ChemComp-UDP:
URIDINE-5'-DIPHOSPHATE / UDP*YM / Uridine diphosphate

ChemComp-TRS:
2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL / pH buffer*YM / Tris

Source
  • thermomyces dupontii (fungus)
KeywordsTRANSFERASE / ENDOPLASMIC RETICULUM / QUALITY CONTROL / GLUCOSYLTRANSFERASE / FOLDING SENSOR

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