3q6j | pdb_00003q6j

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

spinqualitylabelsall models 3q6j, resolution 1.92Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3q6j 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, BCT, CO2, COM, FAD, KPC, MG, NAP Related: 2c3d, 1mo9, 1mok Activity: 2-oxopropyl-CoM reductase (carboxylating), with EC number 1.8.1.5 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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. Publication Abstract from PubMed 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. STRUCTURED SUMMARY: 2-KPCCbinds to 2-KPCC by x-ray crystallography (View interaction). Structural basis for carbon dioxide binding by 2-ketopropyl coenzyme M oxidoreductase/carboxylase.,Pandey AS, Mulder DW, Ensign SA, Peters JW FEBS Lett. 2011 Feb 4;585(3):459-64. Epub 2010 Dec 27. PMID:21192936 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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