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Structure paper

TitleStructural and biochemical analysis of Bacillus anthracis prephenate dehydrogenase reveals an unusual mode of inhibition by tyrosine via the ACT domain.
Journal, issue, pagesFebs J., Vol. 287, Page 2235-2255, Year 2020
Publish dateFeb 24, 2017 (structure data deposition date)
AuthorsShabalin, I.G. / Gritsunov, A. / Hou, J. / Slawek, J. / Miks, C.D. / Cooper, D.R. / Minor, W. / Christendat, D.
External linksFebs J. / PubMed:31750992
MethodsX-ray diffraction
Resolution2.01 - 2.75 Å
Structure data

PDB-5uyy:
Crystal structure of prephenate dehydrogenase tyrA from Bacillus anthracis in complex with L-tyrosine
Method: X-RAY DIFFRACTION / Resolution: 2.6 Å

PDB-5v0s:
Crystal structure of the ACT domain of prephenate dehydrogenase tyrA from Bacillus anthracis
Method: X-RAY DIFFRACTION / Resolution: 2.01 Å

PDB-6cxd:
Crystal structure of peptidase B from Yersinia pestis CO92 at 2.75 A resolution
Method: X-RAY DIFFRACTION / Resolution: 2.75 Å

PDB-6u60:
Crystal structure of prephenate dehydrogenase tyrA from Bacillus anthracis in complex with NAD and L-tyrosine
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

Chemicals

ChemComp-TYR:
TYROSINE

ChemComp-HOH:
WATER

ChemComp-SO4:
SULFATE ION

ChemComp-CA:
Unknown entry

ChemComp-PO4:
PHOSPHATE ION

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

Source
  • bacillus anthracis (anthrax bacterium)
  • yersinia pestis co92 (bacteria)
KeywordsOXIDOREDUCTASE / prephenate dehydrogenase / tyrA / Bacillus anthracis / CSGID / Structural Genomics / Center for Structural Genomics of Infectious Diseases / HYDROLASE / peptidase B

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