1X89
Crystal structure of Siderocalin (NGAL, Lipocalin 2) complexed with Carboxymycobactin S
1X89 の概要
エントリーDOI | 10.2210/pdb1x89/pdb |
関連するPDBエントリー | 1X71 1X8U |
分子名称 | Neutrophil gelatinase-associated lipocalin, CARBOXYMYCOBACTIN S (3 entities in total) |
機能のキーワード | lipocalin, siderophore, antimicrobial protein |
由来する生物種 | Homo sapiens (human) |
細胞内の位置 | Secreted : P80188 |
タンパク質・核酸の鎖数 | 3 |
化学式量合計 | 64074.30 |
構造登録者 | Holmes, M.A.,Paulsene, W.,Jide, X.,Ratledge, C.,Strong, R.K. (登録日: 2004-08-17, 公開日: 2005-01-25, 最終更新日: 2024-11-06) |
主引用文献 | Holmes, M.A.,Paulsene, W.,Jide, X.,Ratledge, C.,Strong, R.K. Siderocalin (Lcn 2) Also Binds Carboxymycobactins, Potentially Defending against Mycobacterial Infections through Iron Sequestration Structure, 13:29-41, 2005 Cited by PubMed Abstract: Siderocalin, a member of the lipocalin family of binding proteins, is found in neutrophil granules, uterine secretions, and at markedly elevated levels in serum and synovium during bacterial infection; it is also secreted from epithelial cells in response to inflammation or tumorigenesis. Identification of high-affinity ligands, bacterial catecholate-type siderophores (such as enterochelin), suggested a possible function for siderocalin: an antibacterial agent, complementing the general antimicrobial innate immune system iron-depletion strategy, sequestering iron as ferric siderophore complexes. Supporting this hypothesis, siderocalin is a potent bacteriostatic agent in vitro under iron-limiting conditions and, when knocked out, renders mice remarkably susceptible to bacterial infection. Here we show that siderocalin also binds soluble siderophores of mycobacteria, including M. tuberculosis: carboxymycobactins. Siderocalin employs a degenerate recognition mechanism to cross react with these dissimilar types of siderophores, broadening the potential utility of this innate immune defense. PubMed: 15642259DOI: 10.1016/j.str.2004.10.009 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.1 Å) |
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