5ZKA
Crystal structure of N-acetylneuraminate lyase from Fusobacterium nucleatum complexed with Pyruvate
Summary for 5ZKA
| Entry DOI | 10.2210/pdb5zka/pdb |
| Descriptor | N-acetylneuraminate lyase, 1,2-ETHANEDIOL, TRIETHYLENE GLYCOL, ... (5 entities in total) |
| Functional Keywords | n-acetylneuraminate lyase, sialic acid catabolism, tim-barrel, schiff base, lyase |
| Biological source | Fusobacterium nucleatum subsp. nucleatum ATCC 25586 More |
| Total number of polymer chains | 2 |
| Total formula weight | 68982.71 |
| Authors | Kumar, J.P.,Rao, H.,Nayak, V.,Ramaswamy, S. (deposition date: 2018-03-23, release date: 2018-12-05, Last modification date: 2023-11-22) |
| Primary citation | Kumar, J.P.,Rao, H.,Nayak, V.,Ramaswamy, S. Crystal structures and kinetics of N-acetylneuraminate lyase from Fusobacterium nucleatum Acta Crystallogr F Struct Biol Commun, 74:725-732, 2018 Cited by PubMed Abstract: N-Acetyl-D-neuraminic acid lyase (NanA) catalyzes the breakdown of sialic acid (Neu5Ac) to N-acetyl-D-mannosamine (ManNAc) and pyruvate. NanA plays a key role in Neu5Ac catabolism in many pathogenic and bacterial commensals where sialic acid is available as a carbon and nitrogen source. Several pathogens or commensals decorate their surfaces with sialic acids as a strategy to escape host innate immunity. Catabolism of sialic acid is key to a range of host-pathogen interactions. In this study, atomic resolution structures of NanA from Fusobacterium nucleatum (FnNanA) in ligand-free and ligand-bound forms are reported at 2.32 and 1.76 Å resolution, respectively. F. nucleatum is a Gram-negative pathogen that causes gingival and periodontal diseases in human hosts. Like other bacterial N-acetylneuraminate lyases, FnNanA also shares the triosephosphate isomerase (TIM)-barrel fold. As observed in other homologous enzymes, FnNanA forms a tetramer. In order to characterize the structure-function relationship, the steady-state kinetic parameters of the enzyme are also reported. PubMed: 30387778DOI: 10.1107/S2053230X18012992 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.76 Å) |
Structure validation
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