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TitleStructural basis for substrate recognition and inhibition of prephenate aminotransferase from Arabidopsis.
Journal, issue, pagesPlant J., Vol. 94, Page 304-314, Year 2018
Publish dateJul 28, 2017 (structure data deposition date)
AuthorsHolland, C.K. / Berkovich, D.A. / Kohn, M.L. / Maeda, H. / Jez, J.M.
External linksPlant J. / PubMed:29405514
MethodsX-ray diffraction
Resolution1.398 - 3 Å
Structure data

PDB-5wmh:
Arabidopsis thaliana prephenate aminotransferase
Method: X-RAY DIFFRACTION / Resolution: 3 Å

PDB-5wmi:
Arabidopsis thaliana Prephenate Aminotransferase mutant- T84V
Method: X-RAY DIFFRACTION / Resolution: 2 Å

PDB-5wmk:
Arabidopsis thaliana Prephenate Aminotransferase double mutant- T84V K169V
Method: X-RAY DIFFRACTION / Resolution: 1.398 Å

PDB-5wml:
Arabidopsis thaliana Prephenate Aminotransferase mutant- K306A
Method: X-RAY DIFFRACTION / Resolution: 2.103 Å

Chemicals

ChemComp-PLP:
PYRIDOXAL-5'-PHOSPHATE

ChemComp-HOH:
WATER

ChemComp-AKG:
2-OXOGLUTARIC ACID

ChemComp-MLI:
MALONATE ION

ChemComp-BO3:
BORIC ACID

ChemComp-PMP:
4'-DEOXY-4'-AMINOPYRIDOXAL-5'-PHOSPHATE

ChemComp-GLU:
GLUTAMIC ACID

Source
  • arabidopsis thaliana (thale cress)
KeywordsTRANSFERASE / aminotransferase / PLP-dependent / aspartate aminotransferase

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