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Structure paper

TitleKinetic and structural evidence that Asp-678 plays multiple roles in catalysis by the quinoprotein glycine oxidase.
Journal, issue, pagesJ. Biol. Chem., Vol. 294, Page 17463-17470, Year 2019
Publish dateSep 12, 2019 (structure data deposition date)
AuthorsMamounis, K.J. / Avalos, D. / Yukl, E.T. / Davidson, V.L.
External linksJ. Biol. Chem. / PubMed:31615898
MethodsX-ray diffraction
Resolution1.83 - 2.51 Å
Structure data

PDB-6ubn:
Crystal structure of D678E GoxA bound to glycine
Method: X-RAY DIFFRACTION / Resolution: 2.15 Å

PDB-6ubr:
Crystal structure of D678A GoxA bound to glycine at pH 7.5
Method: X-RAY DIFFRACTION / Resolution: 1.96 Å

PDB-6ubz:
Crystal structure of D678A GoxA bound to glycine at pH 5.5
Method: X-RAY DIFFRACTION / Resolution: 1.83 Å

PDB-6uc1:
Crystal structure of D678A GoxA soaked in glycine at pH 7.5
Method: X-RAY DIFFRACTION / Resolution: 2.19 Å

PDB-6ufq:
Crystal structure of D678N GoxA bound to glycine
Method: X-RAY DIFFRACTION / Resolution: 2.51 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-NA:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-SO4:
SULFATE ION

ChemComp-PEG:
DI(HYDROXYETHYL)ETHER

ChemComp-GLY:
GLYCINE

ChemComp-PGE:
TRIETHYLENE GLYCOL

Source
  • pseudoalteromonas luteoviolacea dsm 6061 (bacteria)
KeywordsOXIDOREDUCTASE / tryotiophylquinone / oxidase

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