3Q6J

Structural basis for carbon dioxide binding by 2-ketopropyl coenzyme M Oxidoreductase/Carboxylase

Summary for 3Q6J

• Entry DOI: 10.2210/pdb3q6j/pdb
• Related: 1MO9 1MOK 2C3D
• Descriptor: 2-oxopropyl-CoM reductase, carboxylating, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, FLAVIN-ADENINE DINUCLEOTIDE, ... (10 entities in total)
• Functional Keywords: disulfide, carbon dioxide, coenzyme m, fad, nadp, oxidoreductase, carboxylase
• Biological source: Xanthobacter autotrophicus
• Total number of polymer chains: 2
• Total formula weight: 118499.80

Authors

Pandey, A.S.,Mulder, D.W.,Ensign, S.A.,Peters, J.W. (deposition date: 2011-01-01, release date: 2011-02-16, Last modification date: 2023-09-13)

Primary citation

Pandey, A.S.,Mulder, D.W.,Ensign, S.A.,Peters, J.W.
Structural basis for carbon dioxide binding by 2-ketopropyl coenzyme M oxidoreductase/carboxylase.
Febs Lett., 585:459-464, 2011

PubMed Abstract: The structure of 2-ketopropyl coenzyme M oxidoreductase/carboxylase (2-KPCC) has been determined in a state in which CO(2) is observed providing insights into the mechanism of carboxylation. In the substrate encapsulated state of the enzyme, CO(2) is bound at the base of a narrow hydrophobic substrate access channel. The base of the channel is demarcated by a transition from a hydrophobic to hydrophilic environment where CO(2) is located in position for attack on the carbanion of the ketopropyl group of the substrate to ultimately produce acetoacetate. This binding mode effectively discriminates against H(2)O and prevents protonation of the ketopropyl leaving group.

PubMed: 21192936
DOI: 10.1016/j.febslet.2010.12.035

Experimental method

X-RAY DIFFRACTION (1.92 Å)