3DFI

The crystal structure of antimicrobial reagent A40926 pseudoaglycone deacetylase Dbv21

Summary for 3DFI

• Entry DOI: 10.2210/pdb3dfi/pdb
• Related: 3DFF 3DFK 3DFM
• Descriptor: Pseudoaglycone deacetylase Dbv21, ZINC ION (3 entities in total)
• Functional Keywords: single alpha-beta domain, hydrolase
• Biological source: Actinoplanes teichomyceticus
• Total number of polymer chains: 1
• Total formula weight: 29890.78

Authors

Zou, Y.,Brunzelle, J.S.,Nair, S.K. (deposition date: 2008-06-12, release date: 2008-07-22, Last modification date: 2024-02-21)

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

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

Experimental method

X-RAY DIFFRACTION (2.1 Å)