5awv | pdb_00005awv

Crystal structure of glycopeptide hexose oxidase DBV29 complexed with teicoplanin

spinqualitylabelsall models 5awv, resolution 1.93Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5awv is a 12 chain structure with sequence from Actinoplanes teichomyceticus and Nonomuraea gerenzanensis. This structure supersedes the now removed PDB entries 4k3t and 2wdx. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.93Å Ligands: 3FG, 3MY, CIT, FAD, GHP, MAN, N1L, NAG, OMY, T55 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q7WZ62_9ACTN Publication Abstract from PubMed In the search for new efficacious antibiotics, biosynthetic engineering offers attractive opportunities to introduce minor alterations to antibiotic structures that may overcome resistance. Dbv29, a flavin-containing oxidase, catalyzes the four-electron oxidation of a vancomycin-like glycopeptide to yield A40926. Structural and biochemical examination of Dbv29 now provides insights into residues that govern flavinylation and activity, protein conformation and reaction mechanism. In particular, the serendipitous discovery of a reaction intermediate in the crystal structure led us to identify an unexpected opportunity to intercept the normal enzyme mechanism at two different points to create new teicoplanin analogs. Using this method, we synthesized families of antibiotic analogs with amidated and aminated lipid chains, some of which showed marked potency and efficacy against multidrug resistant pathogens. This method offers a new strategy for the development of chemical diversity to combat antibacterial resistance. Interception of teicoplanin oxidation intermediates yields new antimicrobial scaffolds.,Liu YC, Li YS, Lyu SY, Hsu LJ, Chen YH, Huang YT, Chan HC, Huang CJ, Chen GH, Chou CC, Tsai MD, Li TL Nat Chem Biol. 2011 May;7(5):304-9. Epub 2011 Apr 10. PMID:21478878 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA