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TitleStructural and mutational analyses of the bifunctional arginine dihydrolase and ornithine cyclodeaminase AgrE from the cyanobacteriumAnabaena.
Journal, issue, pagesJ. Biol. Chem., Vol. 295, Page 5751-5760, Year 2020
Publish dateJan 16, 2020 (structure data deposition date)
AuthorsLee, H. / Rhee, S.
External linksJ. Biol. Chem. / PubMed:32198136
MethodsX-ray diffraction
Resolution2.0546605257 - 2.70510472826 Å
Structure data

PDB-6lrf:
Crystal structure of unliganded AgrE
Method: X-RAY DIFFRACTION / Resolution: 2.0546605257 Å

PDB-6lrg:
Crystal Structure of the Ternary Complex of AgrE with Ornithine and NAD+
Method: X-RAY DIFFRACTION / Resolution: 2.4121811586 Å

PDB-6lrh:
Crystal Structure of the Binary Complex of AgrE C264A mutant with L-arginine
Method: X-RAY DIFFRACTION / Resolution: 2.70510472826 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-NAD:
NICOTINAMIDE-ADENINE-DINUCLEOTIDE / NAD*YM

ChemComp-ORN:
L-ornithine

ChemComp-ARG:
ARGININE

Source
  • nostoc sp. (strain pcc 7120 / sag 25.82 / utex 2576) (bacteria)
KeywordsHYDROLASE / arginine dihydrolase / bifunctional enzyme / GME family

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