2jkb | pdb_00002jkb

CRYSTAL STRUCTURE OF STREPTOCOCCUS PNEUMONIAE NANB IN COMPLEX WITH 2,7-ANHYDRO-NEU5AC

spinqualitylabelsall models 2jkb, resolution 1.54Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2jkb is a 1 chain structure with sequence from Strpn. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: EDO, SKD Related: 2vw0, 2vw1, 2vw2 Activity: Anhydrosialidase, with EC number 4.2.2.15 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. Structural and functional studies of Streptococcus pneumoniae neuraminidase B: An intramolecular trans-sialidase.,Gut H, King SJ, Walsh MA FEBS Lett. 2008 Oct 15;582(23-24):3348-52. Epub 2008 Sep 5. PMID:18775704 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Neuraminidase

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