3DFF
The crystal structure of teicoplanin pseudoaglycone deacetylase Orf2
Summary for 3DFF
Entry DOI | 10.2210/pdb3dff/pdb |
Related | 3DFI 3DFK 3DFM |
Descriptor | Teicoplanin pseudoaglycone deacetylases Orf2, ZINC ION, TETRAETHYLENE GLYCOL, ... (5 entities in total) |
Functional Keywords | deacetylase, lipoglycopeptide, pseudoaglycone, zinc dependent, hydrolase |
Biological source | Actinoplanes teichomyceticus |
Total number of polymer chains | 1 |
Total formula weight | 30646.76 |
Authors | Zou, Y.,Brunzelle, J.S.,Nair, S.K. (deposition date: 2008-06-11, release date: 2008-07-22, Last modification date: 2024-11-20) |
Primary citation | Zou, Y.,Brunzelle, J.S.,Nair, S.K. Crystal structures of lipoglycopeptide antibiotic deacetylases: implications for the biosynthesis of a40926 and teicoplanin. Chem.Biol., 15:533-545, 2008 Cited by PubMed Abstract: The lipoglycopeptide antibiotics teicoplanin and A40926 have proven efficacy against Gram-positive pathogens. These drugs are distinguished from glycopeptide antibiotics by N-linked long chain acyl-D-glucosamine decorations that contribute to antibacterial efficacy. During the biosynthesis of lipoglycopeptides, tailoring glycosyltransferases attach an N-acetyl-D-glucosamine to the aglycone, and this N-acetyl-glucosaminyl pseudoaglycone is deacetylated prior to long chain hydrocarbon attachment. Here we present several high-resolution crystal structures of the pseudoaglycone deacetylases from the biosynthetic pathways of teicoplanin and A40926. The cocrystal structure of the teicoplanin pseudoaglycone deacetylase with a fatty acid product provides further insights into the roles of active-site residues, and suggests mechanistic similarities with structurally distinct zinc deacetylases, such as peptidoglycan deacetylase and LpxC. A unique, structurally mobile capping lid, located at the apex of these pseudoaglycone deacetylases, likely serves as a determinant of substrate specificity. PubMed: 18559264DOI: 10.1016/j.chembiol.2008.05.009 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.6 Å) |
Structure validation
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