4HZU

Structure of a bacterial energy-coupling factor transporter

4HZU の概要

• エントリーDOI: 10.2210/pdb4hzu/pdb
• 分子名称: Energy-coupling factor transporter ATP-binding protein EcfA 1, Energy-coupling factor transporter ATP-binding protein EcfA 2, Energy-coupling factor transporter transmembrane protein EcfT, ... (4 entities in total)
• 機能のキーワード: membrane protein, ecf, transporter, hydrolase, transport protein
• 由来する生物種: Lactobacillus brevis; 詳細
• 細胞内の位置: Cell membrane; Peripheral membrane protein (By similarity): Q03PY6 Q03PY5; Cell membrane; Multi-pass membrane protein (Potential): Q03PY7
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 110457.11

構造登録者

Wang, T.L.,Fu, G.B.,Pan, X.J.,Shi, Y.G. (登録日: 2012-11-15, 公開日: 2013-04-17, 最終更新日: 2024-02-28)

主引用文献

Wang, T.,Fu, G.,Pan, X.,Wu, J.,Gong, X.,Wang, J.,Shi, Y.
Structure of a bacterial energy-coupling factor transporter.
Nature, 497:272-276, 2013

PubMed Abstract: The energy-coupling factor (ECF) transporters constitute a novel family of conserved membrane transporters in prokaryotes that have a similar domain organization to the ATP-binding cassette transporters. Each ECF transporter comprises a pair of cytosolic ATPases (the A and A' components, or EcfA and EcfA'), a membrane-embedded substrate-binding protein (the S component, or EcfS) and a transmembrane energy-coupling component (the T component, or EcfT) that links the EcfA-EcfA' subcomplex to EcfS. The structure and transport mechanism of the quaternary ECF transporter remain largely unknown. Here we report the crystal structure of a nucleotide-free ECF transporter from Lactobacillus brevis at a resolution of 3.5 Å. The T component has a horseshoe-shaped open architecture, with five α-helices as transmembrane segments and two cytoplasmic α-helices as coupling modules connecting to the A and A' components. Strikingly, the S component, thought to be specific for hydroxymethyl pyrimidine, lies horizontally along the lipid membrane and is bound exclusively by the five transmembrane segments and the two cytoplasmic helices of the T component. These structural features suggest a plausible working model for the transport cycle of the ECF transporters.

PubMed: 23584587
DOI: 10.1038/nature12045

実験手法

X-RAY DIFFRACTION (3.53 Å)