3P7I

Crystal structure of Escherichia coli PhnD in complex with 2-aminoethyl phosphonate

3P7I の概要

• エントリーDOI: 10.2210/pdb3p7i/pdb
• 分子名称: PhnD, subunit of alkylphosphonate ABC transporter, (2-aminoethyl)phosphonic acid, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: phosphonate binding protein, transport protein
• 由来する生物種: Escherichia coli UTI89
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 36209.79

構造登録者

Alicea, I.,Schreiter, E.R. (登録日: 2010-10-12, 公開日: 2011-10-12, 最終更新日: 2024-02-21)

主引用文献

Alicea, I.,Marvin, J.S.,Miklos, A.E.,Ellington, A.D.,Looger, L.L.,Schreiter, E.R.
Structure of the Escherichia coli Phosphonate Binding Protein PhnD and Rationally Optimized Phosphonate Biosensors.
J.Mol.Biol., 414:356-369, 2011

PubMed Abstract: The phnD gene of Escherichia coli encodes the periplasmic binding protein of the phosphonate (Pn) uptake and utilization pathway. We have crystallized and determined structures of E. coli PhnD (EcPhnD) in the absence of ligand and in complex with the environmentally abundant 2-aminoethylphosphonate (2AEP). Similar to other bacterial periplasmic binding proteins, 2AEP binds near the center of mass of EcPhnD in a cleft formed between two lobes. Comparison of the open, unliganded structure with the closed 2AEP-bound structure shows that the two lobes pivot around a hinge by ~70° between the two states. Extensive hydrogen bonding and electrostatic interactions stabilize 2AEP, which binds to EcPhnD with low nanomolar affinity. These structures provide insight into Pn uptake by bacteria and facilitated the rational design of high signal-to-noise Pn biosensors based on both coupled small-molecule dyes and autocatalytic fluorescent proteins.

PubMed: 22019591
DOI: 10.1016/j.jmb.2011.09.047

実験手法

X-RAY DIFFRACTION (1.71 Å)