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2JKB

Crystal structure of Streptococcus pneumoniae NanB in complex with 2, 7-anhydro-Neu5Ac

Summary for 2JKB
Entry DOI10.2210/pdb2jkb/pdb
Related2VW0 2VW1 2VW2
DescriptorSIALIDASE 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 Keywordsintramolecular trans-sialidase, lyase, glycosidase, neuraminidase
Biological sourceSTREPTOCOCCUS PNEUMONIAE
Total number of polymer chains1
Total formula weight77404.98
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 citationGut, 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: 18775704
DOI: 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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数据于2025-06-25公开中

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