5zjp | pdb_00005zjp

Structure of N-acetylmannosamine-6-phosphate-2-epimerase from Vibrio cholerae with N-acetylglucosamine-6-phosphate

spinqualitylabelsall models 5zjp, resolution 2.66Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5zjp is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: EDO, PEG, PGE, RFW Activity: N-acylglucosamine-6-phosphate 2-epimerase, with EC number 5.1.3.9 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [A0A2K2UT85_VIBCL] Converts N-acetylmannosamine-6-phosphate (ManNAc-6-P) to N-acetylglucosamine-6-phosphate (GlcNAc-6-P).[HAMAP-Rule:MF_01235][SAAS:SAAS00761217] Publication Abstract from PubMed 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 A resolution, respectively. The structure of NanE from Fn (FnNanE) has been determined to 2.2 A 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. Crystal structures and kinetic analyses of N-acetylmannosamine-6-phosphate 2-epimerases from Fusobacterium nucleatum and Vibrio cholerae.,Manjunath L, Guntupalli SR, Currie MJ, North RA, Dobson RCJ, Nayak V, Subramanian R Acta Crystallogr F Struct Biol Commun. 2018 Jul 1;74(Pt 7):431-440. doi:, 10.1107/S2053230X18008543. Epub 2018 Jun 28. PMID:29969107 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA