1Y9U
Bordetella ferric binding protein
1Y9U の概要
エントリーDOI | 10.2210/pdb1y9u/pdb |
分子名称 | putative iron binding protein (2 entities in total) |
機能のキーワード | periplasmic binding protein, iron tyrosinate interaction, metal binding protein |
由来する生物種 | Bordetella pertussis Tohama I |
タンパク質・核酸の鎖数 | 1 |
化学式量合計 | 34821.57 |
構造登録者 | Tom-Yew, S.A.L.,Cui, D.T.,Bekker, E.G.,Murphy, M.E.P. (登録日: 2004-12-16, 公開日: 2005-01-11, 最終更新日: 2024-10-30) |
主引用文献 | Tom-Yew, S.A.L.,Cui, D.T.,Bekker, E.G.,Murphy, M.E.P. Anion-independent iron coordination by the Campylobacter jejuni ferric binding protein J.Biol.Chem., 280:9283-9290, 2005 Cited by PubMed Abstract: Campylobacter jejuni, the leading cause of human gastroenteritis, expresses a ferric binding protein (cFbpA) that in many pathogenic bacteria functions to acquire iron as part of their virulence repertoire. Recombinant cFbpA is isolated with ferric iron bound from Escherichia coli. The crystal structure of cFbpA reveals unprecedented iron coordination by only five protein ligands. The histidine and one tyrosine are derived from the N-terminal domain, whereas the three remaining tyrosine ligands are from the C-terminal domain. Surprisingly, a synergistic anion present in all other characterized ferric transport proteins is not observed in the cFbpA iron-binding site, suggesting a novel role for this protein in iron uptake. Furthermore, cFbpA is shown to bind iron with high affinity similar to Neisserial FbpA and exhibits an unusual preference for ferrous iron (oxidized subsequently to the ferric form) or ferric iron chelated by oxalate. Sequence and structure analyses reveal that cFbpA is a member of a new class of ferric binding proteins that includes homologs from invasive and intracellular bacteria as well as cyanobacteria. Overall, six classes are defined based on clustering within the tree and by their putative iron coordination. The absence of a synergistic anion in the iron coordination sphere of cFbpA also suggests an alternative model of evolution for FbpA homologs involving an early iron-binding ancestor instead of a requirement for a preexisting anion-binding ancestor. PubMed: 15613474DOI: 10.1074/jbc.M412479200 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (1.39 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