1O7T
Metal nanoclusters bound to the Ferric Binding Protein from Neisseria gonorrhoeae.
1O7T の概要
エントリーDOI | 10.2210/pdb1o7t/pdb |
関連するPDBエントリー | 1D9Y |
分子名称 | IRON BINDING PROTEIN, HF OXO CLUSTER HF5, SMALLEST HF-OXO-PHOSPHATE CLUSTER HF3, ... (5 entities in total) |
機能のキーワード | metal-binding protein, periplasmic ferric binding protein, hafnium, metal-oxo cluster, metal binding protein |
由来する生物種 | NEISSERIA GONORRHOEAE |
タンパク質・核酸の鎖数 | 9 |
化学式量合計 | 313992.53 |
構造登録者 | Alexeev, D.,Zu, H.,Guo, M.,Zhong, W.,Hunter, D.J.B.,Yang, W.,Campopiano, D.J.,Sadler, P.J. (登録日: 2002-11-12, 公開日: 2003-02-27, 最終更新日: 2023-12-13) |
主引用文献 | Alexeev, D.,Zhu, H.,Guo, M.,Zhong, W.,Hunter, D.J.,Yang, W.,Campopiano, D.J.,Sadler, P.J. A novel protein-mineral interface. Nat. Struct. Biol., 10:297-302, 2003 Cited by PubMed Abstract: Transferrins transport Fe3+ and other metal ions in mononuclear-binding sites. We present the first evidence that a member of the transferrin superfamily is able to recognize multi-nuclear oxo-metal clusters, small mineral fragments that are the most abundant forms of many metals in the environment. We show that the ferric ion-binding protein from Neisseria gonorrhoeae (nFbp) readily binds clusters of Fe3+, Ti4+, Zr4+ or Hf4+ in solution. The 1.7 A resolution crystal structure of Hf-nFbp reveals three distinct types of clusters in an open, positively charged cleft between two hinged protein domains. A di-tyrosyl cluster nucleation motif (Tyr195-Tyr196) is situated at the bottom of this cleft and binds either a trinuclear oxo-Hf cluster, which is capped by phosphate, or a pentanuclear cluster, which in turn can be capped with phosphate. This first high-resolution structure of a protein-mineral interface suggests a novel metal-uptake mechanism and provides a model for protein-mediated mineralization/dissimilation, which plays a critical role in geochemical processes. PubMed: 12598891DOI: 10.1038/nsb903 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (1.65 Å) |
構造検証レポート
検証レポート(詳細版)をダウンロード