TY  - JOUR
A1  - Wöhlert, David
A1  - Grötzinger, Maria J.
A1  - Kühlbrandt, Werner
A1  - Yildiz, Özkan
T1  - Mechanism of Na+-dependent citrate transport from the structure of an asymmetrical CitS dimer
T2  - eLife
N2  - The common human pathogen Salmonella enterica takes up citrate as a nutrient via the sodium symporter SeCitS. Uniquely, our 2.5 Å x-ray structure of the SeCitS dimer shows three different conformations of the active protomer. One protomer is in the outside-facing state. Two are in different inside-facing states. All three states resolve the substrates in their respective binding environments. Together with comprehensive functional studies on reconstituted proteoliposomes, the structures explain the transport mechanism in detail. Our results indicate a six-step process, with a rigid-body 31° rotation of a helix bundle that translocates the bound substrates by 16 Å across the membrane. Similar transport mechanisms may apply to a wide variety of related and unrelated secondary transporters, including important drug targets.
KW  - Na+ transport
KW  - biochemistry
KW  - biophysics
KW  - citrate transport
KW  - crystal structure
KW  - membrane protein
KW  - membrane transport
KW  - secondary transport
KW  - structural biology
Y1  - 2015
UR  - http://publikationen.ub.uni-frankfurt.de/frontdoor/index/index/docId/41295
UR  - https://nbn-resolving.org/urn:nbn:de:hebis:30:3-412950
SN  - 2050-084X
N1  - Copyright Wöhlert et al. This article is distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use and redistribution provided that the original author and source are credited.
VL  - 4
IS  - e09375
SP  - 18
PB  - eLife Sciences Publications
CY  - Cambridge
ER  -