TY - JOUR T1 - Crystal structures and kinetics of N-acetylneuraminate lyase from Fusobacterium nucleatum. JF - Acta Crystallogr F Struct Biol Commun Y1 - 2018 A1 - Kumar, Jay Prakash A1 - Rao, Harshvardhan A1 - Nayak, Vinod A1 - Ramaswamy, S KW - Bacterial Proteins KW - Crystallography, X-Ray KW - Fusobacterium nucleatum KW - Hydrogen Bonding KW - Models, Molecular KW - N-Acetylneuraminic Acid KW - Oxo-Acid-Lyases KW - Protein Conformation KW - Protein Folding KW - Pyruvic Acid KW - Schiff Bases KW - Sequence Alignment KW - Tyrosine AB -

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.

VL - 74 IS - Pt 11 ER -