Structure of a bacterial energy-coupling factor transporter.

Saved in:

Bibliographic Details
Title:	Structure of a bacterial energy-coupling factor transporter.
Authors:	Wang, Tingliang, Fu, Guobin, Pan, Xiaojing, Wu, Jianping, Gong, Xinqi, Wang, Jiawei, Shi, Yigong
Source:	Nature. 5/9/2013, Vol. 497 Issue 7448, p272-276. 5p. 4 Diagrams.
Subjects:	Carrier proteins, Membrane transport proteins, ATP-binding cassette transporters, Membrane proteins, Cytoplasm, Protein transport
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. [ABSTRACT FROM AUTHOR]
	Copyright of Nature is the property of Springer Nature and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)
Database:	Psychology and Behavioral Sciences Collection

Description
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. [ABSTRACT FROM AUTHOR]
ISSN:	00280836
DOI:	10.1038/nature12045