4d0q

Hyaluronan Binding Module of the Streptococcal Pneumoniae Hyaluronate Lyase

spinqualitylabelsall models 4d0q, resolution 1.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4d0q 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 Activity: Hyaluronate lyase, with EC number 4.2.2.1 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed For a subset of pathogenic microorganisms, including Streptococcus pneumoniae, the recognition and degradation of host hyaluronan contributes to bacterial spreading through the extracellular matrix and enhancing access to host-cell surfaces. The hyaluronate lyase, Hyl, presented on the surface of S. pneumoniae performs this role. Using glycan microarray screening, affinity electrophoresis, and isothermal titration calorimetry we show that the N-terminal module of Hyl is a hyaluronan-specific carbohydrate-binding module (CBM) and the founding member of CBM family 70. The 1.2 A resolution X-ray crystal structure of CBM70 revealed it to have a beta-sandwich fold similar to other CBMs. The electrostatic properties of the binding site, which was identified by site-directed mutagenesis, are distinct from other CBMs and complementary to its acidic ligand, hyaluronan. Dynamic light scattering and solution small-angle X-ray scattering (SAXS) revealed the full-length Hyl protein to exist as a monomer-dimer mixture in solution. Through a detailed analysis of the SAXS data we report the pseudo-atomic solution structures of the monomer and dimer forms of the full-length multimodular Hyl. Conformational analysis of the Streptococcus pneumoniae hyaluronate lyase and characterization of its hyaluronan-specific carbohydrate-binding module.,Suits MD, Pluvinage B, Law A, Liu Y, Palma AS, Chai W, Feizi T, Boraston AB J Biol Chem. 2014 Aug 6. pii: jbc.M114.578435. PMID:25100731 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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