期刊
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS
卷 74, 期 -, 页码 725-732出版社
INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S2053230X18012992
关键词
N-acetylneuraminate lyase; sialic acid catabolism; enzyme kinetics; Fusobacterium nucleatum
资金
- Institute for Stem Cell Biology and Regenerative Medicine (inStem)
- DBT Indo-Swedish Collaborative Grant [BT/IN/Sweden/06/SR/2017-18]
- DBT B-LIFE grant [BT/PR12422/MED/31/287/2014]
- infra-structure grant for the in-house X-ray Facility at NCBS/inStem [BT/PR5081/INF/22/156/2012]
- Department of Biotechnology [BT/INF/22/SP22660/2017]
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 angstrom resolution, respectively. F. nucleatum is a Gramnegative 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.
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