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Structure paper

TitleStructural analysis reveals a pyruvate-binding activator site in theAgrobacterium tumefaciensADP-glucose pyrophosphorylase.
Journal, issue, pagesJ. Biol. Chem., Vol. 294, Page 1338-1348, Year 2019
Publish dateJun 15, 2017 (structure data deposition date)
AuthorsHill, B.L. / Mascarenhas, R. / Patel, H.P. / Asencion Diez, M.D. / Wu, R. / Iglesias, A.A. / Liu, D. / Ballicora, M.A.
External linksJ. Biol. Chem. / PubMed:30401744
MethodsX-ray diffraction
Resolution1.754 - 1.78 Å
Structure data

PDB-5w5r:
Agrobacterium tumefaciens ADP-glucose pyrophosphorylase P96A mutant bound to activator pyruvate
Method: X-RAY DIFFRACTION / Resolution: 1.754 Å

PDB-5w5t:
Agrobacterium tumefaciens ADP-Glucose Pyrophosphorylase bound to activator ethyl pyruvate
Method: X-RAY DIFFRACTION / Resolution: 1.76 Å

PDB-5w6j:
Agrobacterium tumefaciens ADP-glucose pyrophosphorylase
Method: X-RAY DIFFRACTION / Resolution: 1.78 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-PYR:
PYRUVIC ACID

ChemComp-HOH:
WATER

ChemComp-GOL:
GLYCEROL

ChemComp-9X7:
ethyl 2-oxopropanoate

Source
  • rhizobium radiobacter (Agrobacterium genomosp. 4)
KeywordsTRANSFERASE / Glucose-1-phosphate adenylyltransferase / glycogen biosynthesis / starch biosynthesis / allosterism

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