4fc4

FNT family ion channel

spinqualitylabelsall models 4fc4, resolution 2.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4fc4 is a 10 chain structure with sequence from Salmonella enterica subsp. enterica serovar Typhimurium str. ST4/74. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: BOG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function E8XEH9_SALT4 Publication Abstract from PubMed Nitrite (NO(2)(-)) is a central intermediate in the nitrogen metabolism of microorganisms and plants, and is used as a cytotoxin by macrophages as part of the innate immune response. The bacterial membrane protein NirC acts as a specific channel to facilitate the transport of nitrite anions across lipid bilayers for cytoplasmic detoxification. Despite NirC's importance in nitrogen metabolism and in the pathogenicity of enteric bacteria, available biochemical data are scarce. Here we present a functional and structural characterization of NirC from Salmonella typhimurium by lipid bilayer electrophysiology and X-ray crystallography. NirC is a pentameric member of the formate/nitrite transporter family of membrane proteins that operates as a channel with high conductance. Single-channel measurements reveal fast and slow gating events but, in contrast to the related FocA formate channel, no pH-dependent gating. A 2.4A crystal structure of NirC at pH 5 shows similarity to FocA and aquaporins, but lacks the structural asymmetry observed in the formate channel at similarly low pH. Resolved water molecules in the protomers suggest a transport mechanism that also permits a facultative NO(2)(-)/H(+) symport. Structural and functional characterization of the nitrite channel NirC from Salmonella typhimurium.,Lu W, Schwarzer NJ, Du J, Gerbig-Smentek E, Andrade SL, Einsle O Proc Natl Acad Sci U S A. 2012 Nov 6;109(45):18395-400. doi:, 10.1073/pnas.1210793109. Epub 2012 Oct 22. PMID:23090993 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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