5ZJM

Crystal structure of N-acetylneuraminate lyase from Fusobacterium nucleatum

Summary for 5ZJM

• Entry DOI: 10.2210/pdb5zjm/pdb
• Descriptor: N-acetylneuraminate lyase, 1,2-ETHANEDIOL (3 entities in total)
• Functional Keywords: n-acetylneuraminate lyase; sialic acid catabolism; tim-barrel, lyase
• Biological source: Fusobacterium nucleatum subsp. nucleatum ATCC 25586
• Total number of polymer chains: 4
• Total formula weight: 131918.45

Authors

Kumar, J.P.,Rao, H.,Nayak, V.,Subramanian, R. (deposition date: 2018-03-21, release date: 2019-01-23, 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

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: 30387778
DOI: 10.1107/S2053230X18012992

Experimental method

X-RAY DIFFRACTION (2.323 Å)