3NRP
Crystal structure of 'as isolated' uropathogenic E. coli strain F11 FetP recombinantly expressed in the periplasm of E. coli BL21(DE3)
3NRP の概要
| エントリーDOI | 10.2210/pdb3nrp/pdb |
| 関連するPDBエントリー | 3NRQ |
| 分子名称 | Periplasmic protein-probably involved in high-affinity Fe2+ transport (2 entities in total) |
| 機能のキーワード | immunoglobulin-like fold, iron transporter, copper binding, transport protein |
| 由来する生物種 | Escherichia coli |
| タンパク質・核酸の鎖数 | 4 |
| 化学式量合計 | 70643.78 |
| 構造登録者 | |
| 主引用文献 | Koch, D.,Chan, A.C.,Murphy, M.E.,Lilie, H.,Grass, G.,Nies, D.H. Characterization of a Dipartite Iron Uptake System from Uropathogenic Escherichia coli Strain F11. J.Biol.Chem., 286:25317-25330, 2011 Cited by PubMed Abstract: In the uropathogenic Escherichia coli strain F11, in silico genome analysis revealed the dicistronic iron uptake operon fetMP, which is under iron-regulated control mediated by the Fur regulator. The expression of fetMP in a mutant strain lacking known iron uptake systems improved growth under iron depletion and increased cellular iron accumulation. FetM is a member of the iron/lead transporter superfamily and is essential for iron uptake by the Fet system. FetP is a periplasmic protein that enhanced iron uptake by FetM. Recombinant FetP bound Cu(II) and the iron analog Mn(II) at distinct sites. The crystal structure of the FetP dimer reveals a copper site in each FetP subunit that adopts two conformations: CuA with a tetrahedral geometry composed of His(44), Met(90), His(97), and His(127), and CuB, a second degenerate octahedral geometry with the addition of Glu(46). The copper ions of each site occupy distinct positions and are separated by ∼1.3 Å. Nearby, a putative additional Cu(I) binding site is proposed as an electron source that may function with CuA/CuB displacement to reduce Fe(III) for transport by FetM. Together, these data indicate that FetMP is an additional iron uptake system composed of a putative iron permease and an iron-scavenging and potentially iron-reducing periplasmic protein. PubMed: 21596746DOI: 10.1074/jbc.M111.222745 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.6 Å) |
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