Volume 52, Issue 40 pp. 10422-10424
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The Tricky Task of Nitrate/Nitrite Antiport

Prof. Susana L. A. Andrade

Prof. Susana L. A. Andrade

Institut für Biochemie, Albert-Ludwigs-Universität Freiburg, Albertstrasse 21, 79104 Freiburg (Germany) http://www.xray.uni-freiburg.de

BIOSS Centre for Biological Signalling Studies, Hebelstrasse 25, 79104 Freiburg (Germany)

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Prof. Oliver Einsle

Corresponding Author

Prof. Oliver Einsle

Institut für Biochemie, Albert-Ludwigs-Universität Freiburg, Albertstrasse 21, 79104 Freiburg (Germany) http://www.xray.uni-freiburg.de

BIOSS Centre for Biological Signalling Studies, Hebelstrasse 25, 79104 Freiburg (Germany)

Institut für Biochemie, Albert-Ludwigs-Universität Freiburg, Albertstrasse 21, 79104 Freiburg (Germany) http://www.xray.uni-freiburg.deSearch for more papers by this author
First published: 09 August 2013
Citations: 3

We thank the Deutsche Forschungsgemeinschaft and the European Research Council for support.

Graphical Abstract

Subtle differences: Two recent crystal structures have provided the first insight into nitrate/nitrite exchangers (example shown with bound nitrite), which are crucial to bacterial metabolism. A direct comparison of the structures reveals how the proteins can distinguish between their highly similar substrates and translate this into a conformational change to translocate ions across the membrane.

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