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TitleBifunctional Substrate Activation via an Arginine Residue Drives Catalysis in Chalcone Isomerases
Journal, issue, pagesAcs Catalysis, Year 2019
Publish dateFeb 26, 2018 (structure data deposition date)
AuthorsBurke, J.R. / La Clair, J.J. / Philippe, R.N. / Pabis, A. / Jez, J.M. / Cortina, G. / Kaltenbach, M. / Bowman, M.E. / Woods, K.B. / Nelson, A.T. ...Burke, J.R. / La Clair, J.J. / Philippe, R.N. / Pabis, A. / Jez, J.M. / Cortina, G. / Kaltenbach, M. / Bowman, M.E. / Woods, K.B. / Nelson, A.T. / Tawfik, D.S. / Kamerlin, S.C.L. / Noel, J.P.
External linksAcs Catalysis / Search PubMed
MethodsX-ray diffraction
Resolution1.9 - 2.4 Å
Structure data

PDB-6cjn:
Crystal Structure of Chalcone Isomerase from Medicago Sativa with the G95T mutation
Method: X-RAY DIFFRACTION / Resolution: 2.4 Å

PDB-6cjo:
Crystal Structure of Chalcone Isomerase from Medicago Sativa with the G95S mutation.
Method: X-RAY DIFFRACTION / Resolution: 2.4 Å

PDB-6ms8:
Crystal Structure of Chalcone Isomerase from Medicago Truncatula Complexed with (2S) Naringenin
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-HOH:
WATER

ChemComp-NAR:
NARINGENIN

Source
  • medicago sativa (alfalfa)
  • medicago truncatula (barrel medic)
Keywordsplant protein / isomerase / chalcone isomerase / naringenin / flavanone

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