5ZKN

Structure of N-acetylmannosamine-6-phosphate 2-epimerase from Fusobacterium nucleatum

Summary for 5ZKN

• Entry DOI: 10.2210/pdb5zkn/pdb
• Descriptor: Putative N-acetylmannosamine-6-phosphate 2-epimerase, CHLORIDE ION (3 entities in total)
• Functional Keywords: sialic acid catabolic pathway epimerase, isomerase
• Biological source: Fusobacterium nucleatum subsp. nucleatum ATCC 25586
• Total number of polymer chains: 1
• Total formula weight: 26999.29

Authors

Manjunath, L. (deposition date: 2018-03-24, release date: 2018-09-19, Last modification date: 2024-03-27)

Primary citation

Manjunath, L.,Guntupalli, S.R.,Currie, M.J.,North, R.A.,Dobson, R.C.J.,Nayak, V.,Subramanian, R.
Crystal structures and kinetic analyses of N-acetylmannosamine-6-phosphate 2-epimerases from Fusobacterium nucleatum and Vibrio cholerae
Acta Crystallogr F Struct Biol Commun, 74:431-440, 2018

PubMed Abstract: Sialic acids are nine-carbon sugars that are found abundantly on the cell surfaces of mammals as glycoprotein or glycolipid complexes. Several Gram-negative and Gram-positive bacteria have the ability to scavenge and catabolize sialic acids to use as a carbon source. This gives them an advantage in colonizing sialic acid-rich environments. The genes of the sialic acid catabolic pathway are generally present as the operon nanAKE. The third gene in the operon encodes the enzyme N-acetylmannosamine-6-phosphate 2-epimerase (NanE), which catalyzes the conversion of N-acetylmannosamine 6-phosphate to N-acetylglucosamine 6-phosphate, thus committing it to enter glycolysis. The NanE enzyme belongs to the isomerase class of enzymes possessing the triose phosphate isomerase (TIM) barrel fold. Here, comparative structural and functional characterizations of the NanE epimerases from two pathogenic Gram-negative bacteria, Fusobacterium nucleatum (Fn) and Vibrio cholerae (Vc), have been carried out. Structures of NanE from Vc (VcNanE) with and without ligand bound have been determined to 1.7 and 2.7 Å resolution, respectively. The structure of NanE from Fn (FnNanE) has been determined to 2.2 Å resolution. The enzymes show kinetic parameters that are consistent with those of Clostridium perfringens NanE. These studies allowed an evaluation of whether NanE may be a good drug target against these pathogenic bacteria.

PubMed: 29969107
DOI: 10.1107/S2053230X18008543

Experimental method

X-RAY DIFFRACTION (2.205 Å)