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Structure paper

TitleCovalent Modification of the Flavin in Proline Dehydrogenase by Thiazolidine-2-Carboxylate.
Journal, issue, pagesAcs Chem. Biol., Vol. 15, Page 936-944, Year 2020
Publish dateSep 24, 2019 (structure data deposition date)
AuthorsCampbell, A.C. / Becker, D.F. / Gates, K.S. / Tanner, J.J.
External linksAcs Chem. Biol. / PubMed:32159324
MethodsX-ray diffraction
Resolution1.52 - 1.737 Å
Structure data

PDB-6ufp:
Structure of proline utilization A with the FAD covalently modified by L-thiazolidine-2-carboxylate and three cysteines (Cys46, Cys470, Cys638) modified to S,S-(2-HYDROXYETHYL)THIOCYSTEINE
Method: X-RAY DIFFRACTION / Resolution: 1.737 Å

PDB-6vz9:
Structure of proline utilization A with the FAD covalently modified by L-thiazolidine-2-carboxylate
Method: X-RAY DIFFRACTION / Resolution: 1.52 Å

Chemicals

ChemComp-FDA:
DIHYDROFLAVINE-ADENINE DINUCLEOTIDE

ChemComp-T2C:
(2S)-1,3-thiazolidine-2-carboxylic acid

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

ChemComp-PEG:
DI(HYDROXYETHYL)ETHER

ChemComp-SO4:
SULFATE ION

ChemComp-FMT:
FORMIC ACID

ChemComp-HOH:
WATER

ChemComp-FAD:
FLAVIN-ADENINE DINUCLEOTIDE / FAD*YM

ChemComp-MG:
Unknown entry

ChemComp-PGE:
TRIETHYLENE GLYCOL

Source
  • sinorhizobium meliloti (strain sm11) (bacteria)
KeywordsOXIDOREDUCTASE / FLAVOENZYME / ROSSMANN FOLD / PROLINE CATABOLISM / SUBSTRATE CHANNELING / BIFUNCTIONAL ENZYME

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