2c3c

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spinqualitylabelsall models 2c3c, resolution 2.15Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

2.01 ANGSTROM X-RAY CRYSTAL STRUCTURE OF A MIXED DISULFIDE BETWEEN COENZYME M AND NADPH-DEPENDENT OXIDOREDUCTASE 2-KETOPROPYL COENZYME M CARBOXYLASE

Overview

The structure of the mixed, enzyme-cofactor disulfide intermediate of, ketopropyl-coenzyme M oxidoreductase/carboxylase has been determined by, X-ray diffraction methods. Ketopropyl-coenzyme M, oxidoreductase/carboxylase belongs to a family of pyridine, nucleotide-containing flavin-dependent disulfide oxidoreductases, which, couple the transfer of hydride derived from the NADPH to the reduction of, protein cysteine disulfide. Ketopropyl-coenzyme M, oxidoreductase/carboxylase, a unique member of this enzyme class, catalyzes thioether bond cleavage of the substrate, 2-ketopropyl-coenzyme, M, and carboxylation of what is thought to be an enzyme-stabilized, enolacetone intermediate. The mixed disulfide of 2-ketopropyl-coenzyme M, oxidoreductase/carboxylase was captured through crystallization ... [(full description)]

About this Structure

2C3C is a [Single protein] structure of sequence from [Xanthobacter autotrophicus] with COM, FAD, NAP and ACN as [ligands]. Active as [[1]], with EC number [1.8.1.5]. Full crystallographic information is available from [OCA].

Reference

Mechanistic implications of the structure of the mixed-disulfide intermediate of the disulfide oxidoreductase, 2-ketopropyl-coenzyme M oxidoreductase/carboxylase., Pandey AS, Nocek B, Clark DD, Ensign SA, Peters JW, Biochemistry. 2006 Jan 10;45(1):113-20. PMID:16388586

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