Hyaluronan Binding Module of the Streptococcal Pneumoniae Hyaluronate LyaseHyaluronan Binding Module of the Streptococcal Pneumoniae Hyaluronate Lyase

Structural highlights

4d0q is a 1 chain structure with sequence from Streptococcus pneumoniae TIGR4. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.2Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

HYSA_STRPN

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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Suits MD, Pluvinage B, Law A, Liu Y, Palma AS, Chai W, Feizi T, Boraston AB. Conformational analysis of the Streptococcus pneumoniae hyaluronate lyase and characterization of its hyaluronan-specific carbohydrate-binding module. J Biol Chem. 2014 Aug 6. pii: jbc.M114.578435. PMID:25100731 doi:http://dx.doi.org/10.1074/jbc.M114.578435

4d0q, resolution 1.20Å

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