5uos

Crystal Structure of CblC (MMACHC) (1-238), a human B12 processing enzyme, complexed with an Antivitamin B12

spinqualitylabelsall models 5uos, resolution 2.51Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5uos is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.51Å Ligands: 171, 8FS, GSH, NA, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Disease MMAC_HUMAN Methylmalonic acidemia with homocystinuria, type cblC. The disease is caused by mutations affecting the gene represented in this entry. Function MMAC_HUMAN May be involved in the binding and intracellular trafficking of cobalamin (vitamin B12). Publication Abstract from PubMed B12 antivitamins are important and robust tools for investigating the biological roles of vitamin B12 . Here, the potential antivitamin B12 2,4-difluorophenylethynylcobalamin (F2PhEtyCbl) was prepared, and its 3D structure was studied in solution and in the crystal. Chemically inert F2PhEtyCbl resisted thermolysis of its Co-C bond at 100 degrees C, was stable in bright daylight, and also remained intact upon prolonged storage in aqueous solution at room temperature. It binds to the human B12 -processing enzyme CblC with high affinity (KD =130 nm) in the presence of the cosubstrate glutathione (GSH). F2PhEtyCbl withstood tailoring by CblC, and it also stabilized the ternary complex with GSH. The crystal structure of this inactivated assembly provides first insight into the binding interactions between an antivitamin B12 and CblC, as well as into the organization of GSH and a base-off cobalamin in the active site of this enzyme. Antivitamin B12 Inhibition of the Human B12 -Processing Enzyme CblC: Crystal Structure of an Inactive Ternary Complex with Glutathione as the Cosubstrate.,Ruetz M, Shanmuganathan A, Gherasim C, Karasik A, Salchner R, Kieninger C, Wurst K, Banerjee R, Koutmos M, Krautler B Angew Chem Int Ed Engl. 2017 Jun 19;56(26):7387-7392. doi:, 10.1002/anie.201701583. Epub 2017 May 23. PMID:28544088 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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