2X86

AGME bound to ADP-B-mannose

Summary for 2X86

• Entry DOI: 10.2210/pdb2x86/pdb
• Related: 2X6T
• Descriptor: ADP-L-GLYCERO-D-MANNO-HEPTOSE-6-EPIMERASE, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, ADENOSINE-5'-DIPHOSPHATE, ... (5 entities in total)
• Functional Keywords: lipopolysaccharide biosynthesis, carbohydrate metabolism, isomerase, stress response
• Biological source: ESCHERICHIA COLI
• Total number of polymer chains: 20
• Total formula weight: 824665.32

Authors

Kowatz, T.,Morrison, J.P.,Tanner, M.E.,Naismith, J.H. (deposition date: 2010-03-06, release date: 2010-03-16, Last modification date: 2023-12-20)

Primary citation

Kowatz, T.,Morrison, J.P.,Tanner, M.E.,Naismith, J.H.
The Crystal Structure of the Y140F Mutant of Adp-L-Glycero-D-Manno-Heptose 6-Epimerase Bound to Adp-Beta-D-Mannose Suggests a One Base Mechanism.
Protein Sci., 19:1337-, 2010

PubMed Abstract: Bacteria synthesize a wide array of unusual carbohydrate molecules, which they use in a variety of ways. The carbohydrate L-glycero-D-manno-heptose is an important component of lipopolysaccharide and is synthesized in a complex series of enzymatic steps. One step involves the epimerization at the C6'' position converting ADP-D-glycero-D-manno-heptose into ADP-L-glycero-D-manno-heptose. The enzyme responsible is a member of the short chain dehydrogenase superfamily, known as ADP-L-glycero-D-manno-heptose 6-epimerase (AGME). The structure of the enzyme was known but the arrangement of the catalytic site with respect to the substrate is unclear. We now report the structure of AGME bound to a substrate mimic, ADP-beta-D-mannose, which has the same stereochemical configuration as the substrate. The complex identifies the key residues and allows mechanistic insight into this novel enzyme.

PubMed: 20506248
DOI: 10.1002/PRO.410

Experimental method

X-RAY DIFFRACTION (2.8 Å)