Crystal structures and kinetics of N-acetylneuraminate lyase from Fusobacterium nucleatum.
|Title||Crystal structures and kinetics of N-acetylneuraminate lyase from Fusobacterium nucleatum.|
|Publication Type||Journal Article|
|Year of Publication||2018|
|Authors||Kumar JPrakash, Rao H, Nayak V, Ramaswamy S|
|Journal||Acta Crystallogr F Struct Biol Commun|
|Date Published||2018 Nov 01|
|Keywords||Bacterial Proteins, Crystallography, X-Ray, Fusobacterium nucleatum, Hydrogen Bonding, Models, Molecular, N-Acetylneuraminic Acid, Oxo-Acid-Lyases, Protein Conformation, Protein Folding, Pyruvic Acid, Schiff Bases, Sequence Alignment, Tyrosine|
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.
|Alternate Journal||Acta Crystallogr F Struct Biol Commun|
|PubMed Central ID||PMC6213981|
|Grant List||BT/IN/Sweden/41/SR/2013 / / Department of Biotechnology, Government of India / |
BT/PR12422/MED/31/287/214 / / Department of Biotechnology, Government of India /
BT/INF/22/SP22660/2017 / / Department of Biotechnology, Government of India /
BT/PR5081/INF/156/2012 / / Department of Biotechnology, Government of India /
BBT/IN/Sweden/06/SR/2017-18 / / Department of Biotechnology, Government of India /