1C82
MECHANISM OF HYALURONAN BINDING AND DEGRADATION: STRUCTURE OF STREPTOCOCCUS PNEUMONIAE HYALURONATE LYASE IN COMPLEX WITH HYALURONIC ACID DISACCHARIDE AT 1.7 A RESOLUTION
1C82 の概要
| エントリーDOI | 10.2210/pdb1c82/pdb |
| 分子名称 | HYALURONATE LYASE, 4-deoxy-alpha-L-threo-hex-4-enopyranuronic acid-(1-3)-2-acetamido-2-deoxy-beta-D-glucopyranose, CACODYLATE ION, ... (5 entities in total) |
| 機能のキーワード | protein-carbohydrate complex, lyase |
| 由来する生物種 | Streptococcus pneumoniae |
| 細胞内の位置 | Secreted, cell wall; Peptidoglycan-anchor (Potential): Q54873 |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 84640.53 |
| 構造登録者 | |
| 主引用文献 | Ponnuraj, K.,Jedrzejas, M.J. Mechanism of hyaluronan binding and degradation: structure of Streptococcus pneumoniae hyaluronate lyase in complex with hyaluronic acid disaccharide at 1.7 A resolution. J.Mol.Biol., 299:885-895, 2000 Cited by PubMed Abstract: Hyaluronic acid (HA) is an important constituent of the extracellular matrix; its bacterial degradation has been postulated to contribute to the spread of certain streptococci through tissue. Pneumococci and other streptococci produce hyaluronate lyase, an enzyme which depolymerizes HA, thus hyaluronate lyase might contribute directly to bacterial invasion. Although two different mechanisms for lyase action have been proposed, there was no crystallographic evidence to support those mechanisms. Here, we report the high-resolution crystal structure of Streptococcus pneumoniae hyaluronate lyase in the presence of HA disaccharide product, which ultimately provides the first crystallographic evidence for the binding of HA to hyaluronate lyase. This structural complex revealed a key interaction between the Streptococcus peneumoniae hyaluronate lyase protein and the product, and supports our previously proposed novel catalytic mechanism for HA degradation based on the native Streptococcus peneumoniae hyaluronate lyase structure. The information provided by this complex structure will likely be useful in the development of antimicrobial pharmaceutical agents. PubMed: 10843845DOI: 10.1006/jmbi.2000.3817 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.7 Å) |
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