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Crystal Structure of a Group I Energy Coupling Factor Vitamin Transporter S Component in Complex with Its Cognate Substrate.

Abstract：

:Energy coupling factor (ECF) transporters are responsible for the uptake of essential scarce nutrients in prokaryotes. This ATP-binding cassette transporter family comprises two subgroups that share a common architecture forming a tripartite membrane protein complex consisting of a translocation component and ATP hydrolyzing module and a substrate-capture (S) component. Here, we present the crystal structure of YkoE from Bacillus subtilis, the S component of the previously uncharacterized group I ECF transporter YkoEDC. Structural and biochemical analyses revealed the constituent residues of the thiamine-binding pocket as well as an unexpected mode of vitamin recognition. In addition, our experimental and bioinformatics data demonstrate major differences between YkoE and group II ECF transporters and indicate how group I vitamin transporter S components have diverged from other group I and group II ECF transporters.

journal_name

Cell Chem Biol

journal_title

Cell chemical biology

authors

Josts I,Almeida Hernandez Y,Andreeva A,Tidow H

doi

10.1016/j.chembiol.2016.06.008

subject

Has Abstract

pub_date

2016-07-21 00:00:00

pages

827-836

issue

7

eissn

2451-9456

issn

2451-9448

pii

S2451-9456(16)30201-X

journal_volume

23

pub_type

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