1EQ2

THE CRYSTAL STRUCTURE OF ADP-L-GLYCERO-D-MANNOHEPTOSE 6-EPIMERASE

Summary for 1EQ2

• Entry DOI: 10.2210/pdb1eq2/pdb
• Descriptor: ADP-L-GLYCERO-D-MANNOHEPTOSE 6-EPIMERASE, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, ADENOSINE-5'-DIPHOSPHATE-GLUCOSE, ... (4 entities in total)
• Functional Keywords: n-terminal domain rossmann fold, c-terminal mixed alpha/beta domain, short-chain dehydrogenase/reductase fold, isomerase
• Biological source: Escherichia coli
• Total number of polymer chains: 10
• Total formula weight: 362757.78

Authors

Deacon, A.M.,Ni, Y.S.,Coleman Jr., W.G.,Ealick, S.E. (deposition date: 2000-03-31, release date: 2000-11-08, Last modification date: 2024-10-16)

Primary citation

Deacon, A.M.,Ni, Y.S.,Coleman Jr., W.G.,Ealick, S.E.
The crystal structure of ADP-L-glycero-D-mannoheptose 6-epimerase: catalysis with a twist.
Structure Fold.Des., 8:453-462, 2000

PubMed Abstract: ADP-L-glycero--mannoheptose 6-epimerase (AGME) is required for lipopolysaccharide (LPS) biosynthesis in most genera of pathogenic and non-pathogenic Gram-negative bacteria. It catalyzes the interconversion of ADP-D-glycero-D-mannoheptose and ADP-L-glycero-D-mannoheptose, a precursor of the seven-carbon sugar L-glycero-mannoheptose (heptose). Heptose is an obligatory component of the LPS core domain; its absence results in a truncated LPS structure resulting in susceptibility to hydrophobic antibiotics. Heptose is not found in mammalian cells, thus its biosynthetic pathway in bacteria presents a unique target for the design of novel antimicrobial agents.

PubMed: 10896473
DOI: 10.1016/S0969-2126(00)00128-3

Experimental method

X-RAY DIFFRACTION (2 Å)