4D0Q
Hyaluronan Binding Module of the Streptococcal Pneumoniae Hyaluronate Lyase
4D0Q の概要
| エントリーDOI | 10.2210/pdb4d0q/pdb |
| 分子名称 | HYALURONATE LYASE, 1,2-ETHANEDIOL (3 entities in total) |
| 機能のキーワード | lyase, hyaluronan binding carbohydrate binding module, cbm, pl family 8, pl8, hyl |
| 由来する生物種 | STREPTOCOCCUS PNEUMONIAE TIGR4 |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 19606.95 |
| 構造登録者 | Suits, M.D.L.,Pluvinage, B.,Law, A.,Liu, Y.,Palma, A.S.,Chai, W.,Feizi, T.,Boraston, A.B. (登録日: 2014-04-29, 公開日: 2014-08-06, 最終更新日: 2024-05-08) |
| 主引用文献 | 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 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.2 Å) |
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