2c3c | pdb_00002c3c

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

spinqualitylabelsall models 2c3c, resolution 2.15Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2c3c is a 2 chain structure with sequence from Xanthobacter autotrophicus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ACN, COM, FAD, NAP Related: 1mo9, 1mok, 2c3d Activity: 2-oxopropyl-CoM reductase (carboxylating), with EC number 1.8.1.5 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Function [XECC_XANP2] Catalyzes the reductive cleavage of the thioether linkage of 2-ketopropyl-coenzyme M, and the subsequent carboxylation of the ketopropyl cleavage product, yielding the products acetoacetate and free coenzyme M. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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 of the enzyme with the physiological products of the reaction, acetoacetate, coenzyme M, and NADP, and reduction of the crystals with dithiothreitol just prior to data collection. Density in the active-site environment consistent with acetone, the product of reductive decarboxylation of acetoacetate, was revealed in this structure in addition to a well-defined hydrophobic pocket or channel that could be involved in the access for carbon dioxide. The analysis of this structure and that of a coenzyme-M-bound form provides insights into the stabilization of intermediates, substrate carboxylation, and product release. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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