1eyq

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Chalcone isomerase and naringeninChalcone isomerase and naringenin

Structural highlights

1eyq is a 2 chain structure with sequence from Medicago sativa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.85Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CFI1_MEDSA Catalyzes the intramolecular cyclization of bicyclic chalcones into tricyclic (S)-flavanones. Responsible for the isomerization of 4,2',4',6'-tetrahydroxychalcone (also termed chalcone) into naringenin.[1] [2] [3]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

References

  1. Jez JM, Bowman ME, Dixon RA, Noel JP. Structure and mechanism of the evolutionarily unique plant enzyme chalcone isomerase. Nat Struct Biol. 2000 Sep;7(9):786-91. PMID:10966651 doi:10.1038/79025
  2. Jez JM, Bowman ME, Noel JP. Role of hydrogen bonds in the reaction mechanism of chalcone isomerase. Biochemistry. 2002 Apr 23;41(16):5168-76. PMID:11955065
  3. Jez JM, Noel JP. Reaction mechanism of chalcone isomerase. pH dependence, diffusion control, and product binding differences. J Biol Chem. 2002 Jan 11;277(2):1361-9. Epub 2001 Nov 6. PMID:11698411 doi:10.1074/jbc.M109224200

1eyq, resolution 1.85Å

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OCA