The tricky task of nitrate/nitrite antiport.
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.
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).
Susana L A
SL
Andrade
Oliver
O
Einsle
D027321:Anion Transport Proteins / Q000737:chemistry* / Q000378:metabolism*; D004734:Energy Metabolism; D004926:Escherichia coli / Q000378:metabolism*; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000378:metabolism*; D017136:Ion Transport; D008958:Models, Molecular; D000091285:Nitrate Transporters; D009566:Nitrates / Q000737:chemistry / Q000378:metabolism*; D009573:Nitrites / Q000737:chemistry / Q000378:metabolism*; D014961:X-Ray Diffraction
D027321:Anion Transport Proteins; D029968:Escherichia coli Proteins; C463079:NarU protein, E coli; D000091285:Nitrate Transporters; D009566:Nitrates; D009573:Nitrites
X-ray diffraction; bioenergetics; major facilitator family; membrane proteins; nitrogen metabolism