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TitleThe unique Phe-His dyad of 2-ketopropyl coenzyme M oxidoreductase/carboxylase selectively promotes carboxylation and S-C bond cleavage.
Journal, issue, pagesJ. Biol. Chem., Vol. 297, Page 100961-100961, Year 2021
Publish dateApr 12, 2021 (structure data deposition date)
AuthorsPrussia, G.A. / Shisler, K.A. / Zadvornyy, O.A. / Streit, B.R. / DuBois, J.L. / Peters, J.W.
External linksJ. Biol. Chem. / PubMed:34265301
MethodsX-ray diffraction
Resolution1.8 - 1.85 Å
Structure data

PDB-7mgn:
Crystal structure of F501H/H506E variant of 2-ketopropyl coenzyme M oxidoreductase/carboxylase (2-KPCC) from Xanthobacter autotrophicus
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

PDB-7mgo:
Crystal structure of F501H variant of 2-ketopropyl coenzyme M oxidoreductase/carboxylase (2-KPCC) from Xanthobacter autotrophicus
Method: X-RAY DIFFRACTION / Resolution: 1.85 Å

Chemicals

ChemComp-COM:
1-THIOETHANESULFONIC ACID

ChemComp-FDA:
DIHYDROFLAVINE-ADENINE DINUCLEOTIDE

ChemComp-MG:
Unknown entry

ChemComp-HOH:
WATER

Source
  • xanthobacter autotrophicus py2 (bacteria)
KeywordsOXIDOREDUCTASE / carboxylation / oxidation-reduction / carbon dioxide fixation / carbon-carbon bond / anion-binding / kinetics

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