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3DFF

The crystal structure of teicoplanin pseudoaglycone deacetylase Orf2

Summary for 3DFF
Entry DOI10.2210/pdb3dff/pdb
Related3DFI 3DFK 3DFM
DescriptorTeicoplanin pseudoaglycone deacetylases Orf2, ZINC ION, TETRAETHYLENE GLYCOL, ... (5 entities in total)
Functional Keywordsdeacetylase, lipoglycopeptide, pseudoaglycone, zinc dependent, hydrolase
Biological sourceActinoplanes teichomyceticus
Total number of polymer chains1
Total formula weight30646.76
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 citationZou, 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: 18559264
DOI: 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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