4D0Q
Hyaluronan Binding Module of the Streptococcal Pneumoniae Hyaluronate Lyase
Summary for 4D0Q
Entry DOI | 10.2210/pdb4d0q/pdb |
Descriptor | HYALURONATE LYASE, 1,2-ETHANEDIOL (3 entities in total) |
Functional Keywords | lyase, hyaluronan binding carbohydrate binding module, cbm, pl family 8, pl8, hyl |
Biological source | STREPTOCOCCUS PNEUMONIAE TIGR4 |
Total number of polymer chains | 1 |
Total formula weight | 19606.95 |
Authors | Suits, M.D.L.,Pluvinage, B.,Law, A.,Liu, Y.,Palma, A.S.,Chai, W.,Feizi, T.,Boraston, A.B. (deposition date: 2014-04-29, release date: 2014-08-06, Last modification date: 2024-05-08) |
Primary citation | Suits, M.D.L.,Pluvinage, B.,Law, A.,Liu, Y.,Palma, A.S.,Chai, W.,Feizi, T.,Boraston, A.B. Conformational Analysis of the Streptococcus Pneumoniae Hyaluronate Lyase and Characterization of its Hyaluronan-Specific Carbohydrate-Binding Module. J.Biol.Chem., 289:27264-, 2014 Cited by PubMed Abstract: 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 Å resolution x-ray crystal structure of CBM70 revealed it to have a β-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 revealed the full-length Hyl protein to exist as a monomer/dimer mixture in solution. Through a detailed analysis of the small angle x-ray scattering data, we report the pseudoatomic solution structures of the monomer and dimer forms of the full-length multimodular Hyl. PubMed: 25100731DOI: 10.1074/JBC.M114.578435 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.2 Å) |
Structure validation
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