3vew | pdb_00003vew

Crystal structure of the O-carbamoyltransferase TobZ in complex with ADP

spinqualitylabelsall models 3vew, resolution 2.35Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3vew is a 1 chain structure with sequence from Streptoalloteichus tenebrarius. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ADP, FE2, SO4 Related: 3ven, 3veo, 3ver, 3ves, 3vet, 3vex, 3vez, 3vf2, 3vf4 Gene: tacA, tobZ (Streptoalloteichus tenebrarius) Resources: FirstGlance, OCA, RCSB, PDBsum Function [Q70IY1_STRSD] TobZ is involved in the biosynthesis of the 2-deoxystreptamine-containing aminoglycoside antibiotics such as nebramycin 5 and 6-O-carbamoylkanamycin. Catalyzes the hydrolysis of carbamoyl phosphate and its subsequent adenylation by ATP to yield O-carbamoyladenylate. Then it catalyzes the transfer of the carbamoyl moiety from O-carbamoyladenylate to the tobramycin 6-hydroxy group to yield nebramycin 5. It catalyzes the same reaction with kanamycin A. These reactions are considerably slower in the presence of deoxy-ATP. Publication Abstract from PubMed An ancient reaction vessel: TobZ carbamoylates the antibiotic tobramycin to form nebramycin 5'. The YrdC-like domain (blue) catalyzes the formation of the novel intermediate carbamoyladenylate, which is channeled through a common "reaction chamber" to the Kae1-like domain (brown), site of carbamoyl transfer. The O-Carbamoyltransferase TobZ Catalyzes an Ancient Enzymatic Reaction.,Parthier C, Gorlich S, Jaenecke F, Breithaupt C, Brauer U, Fandrich U, Clausnitzer D, Wehmeier UF, Bottcher C, Scheel D, Stubbs MT Angew Chem Int Ed Engl. 2012 Mar 1. doi: 10.1002/anie.201108896. PMID:22383337 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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