2JKB
Crystal structure of Streptococcus pneumoniae NanB in complex with 2, 7-anhydro-Neu5Ac
Summary for 2JKB
Entry DOI | 10.2210/pdb2jkb/pdb |
Related | 2VW0 2VW1 2VW2 |
Descriptor | SIALIDASE B, 2-ACETYLAMINO-7-(1,2-DIHYDROXY-ETHYL)-3-HYDROXY-6,8-DIOXA-BICYCLO[3.2.1]OCTANE-5-CARBOXYLIC ACID, 1,2-ETHANEDIOL, ... (4 entities in total) |
Functional Keywords | intramolecular trans-sialidase, lyase, glycosidase, neuraminidase |
Biological source | STREPTOCOCCUS PNEUMONIAE |
Total number of polymer chains | 1 |
Total formula weight | 77404.98 |
Authors | Gut, H.,King, S.J.,Walsh, M.A. (deposition date: 2008-08-26, release date: 2008-09-16, Last modification date: 2024-05-01) |
Primary citation | Gut, H.,King, S.J.,Walsh, M.A. Structural and Functional Studies of Streptococcus Pneumoniae Neuraminidase B: An Intramolecular Trans-Sialidase. FEBS Lett., 582:3348-, 2008 Cited by PubMed Abstract: The human pathogen Streptococcus pneumoniae expresses neuraminidase proteins that cleave sialic acids from complex carbohydrates. The pneumococcus genome encodes up to three neuraminidase proteins that have been shown to be important virulence factors. Here, we report the first structure of a neuraminidase from S. pneumoniae: the crystal structure of NanB in complex with its reaction product 2,7-anhydro-Neu5Ac. Our structural data, together with biochemical analysis, establish NanB as an intramolecular trans-sialidase with strict specificity towards alpha2-3 linked sialic acid substrates. In addition, we show that NanB differs in its substrate specificity from the other pneumococcal neuraminidase NanA. PubMed: 18775704DOI: 10.1016/J.FEBSLET.2008.08.026 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.54 Å) |
Structure validation
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