7MGO

Crystal structure of F501H variant of 2-ketopropyl coenzyme M oxidoreductase/carboxylase (2-KPCC) from Xanthobacter autotrophicus

Summary for 7MGO

• Entry DOI: 10.2210/pdb7mgo/pdb
• Related: 7MGN
• Descriptor: 2-oxopropyl-CoM reductase, carboxylating, DIHYDROFLAVINE-ADENINE DINUCLEOTIDE, 1-THIOETHANESULFONIC ACID, ... (5 entities in total)
• Functional Keywords: carboxylation, oxidation-reduction, carbon dioxide fixation, carbon-carbon bond, anion-binding, kinetics, oxidoreductase
• Biological source: Xanthobacter autotrophicus Py2
• Total number of polymer chains: 2
• Total formula weight: 116718.77

Authors

Prussia, G.,Zadvornyy, O.A.,Peters, J.W. (deposition date: 2021-04-13, release date: 2021-07-21, Last modification date: 2023-10-18)

• Primary citation: Prussia, G.A.,Shisler, K.A.,Zadvornyy, O.A.,Streit, B.R.,DuBois, J.L.,Peters, J.W.; The unique Phe-His dyad of 2-ketopropyl coenzyme M oxidoreductase/carboxylase selectively promotes carboxylation and S-C bond cleavage.; J.Biol.Chem., 297:100961-100961, 2021; PubMed: 34265301; DOI: 10.1016/j.jbc.2021.100961

Experimental method

X-RAY DIFFRACTION (1.85 Å)