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4fc4

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==FNT family ion channel==
==FNT family ion channel==
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<StructureSection load='4fc4' size='340' side='right' caption='[[4fc4]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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<StructureSection load='4fc4' size='340' side='right'caption='[[4fc4]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4fc4]] is a 10 chain structure with sequence from [http://en.wikipedia.org/wiki/Salt4 Salt4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FC4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4FC4 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4fc4]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_Typhimurium_str._ST4/74 Salmonella enterica subsp. enterica serovar Typhimurium str. ST4/74]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FC4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FC4 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BOG:B-OCTYLGLUCOSIDE'>BOG</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3q7k|3q7k]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BOG:B-OCTYLGLUCOSIDE'>BOG</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">nirC, STM474_3643 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=909946 SALT4])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4fc4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fc4 OCA], [https://pdbe.org/4fc4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fc4 RCSB], [https://www.ebi.ac.uk/pdbsum/4fc4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fc4 ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4fc4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fc4 OCA], [http://pdbe.org/4fc4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4fc4 RCSB], [http://www.ebi.ac.uk/pdbsum/4fc4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4fc4 ProSAT]</span></td></tr>
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</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/E8XEH9_SALT4 E8XEH9_SALT4]
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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.
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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<ref>PMID:23090993</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4fc4" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Salt4]]
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[[Category: Large Structures]]
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[[Category: Andrade, S L.A]]
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[[Category: Salmonella enterica subsp. enterica serovar Typhimurium str. ST4/74]]
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[[Category: Du, J]]
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[[Category: Andrade SLA]]
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[[Category: Einsle, O]]
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[[Category: Du J]]
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[[Category: Gerbig-Smentek, E]]
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[[Category: Einsle O]]
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[[Category: Lue, W]]
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[[Category: Gerbig-Smentek E]]
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[[Category: Schwarzer, N]]
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[[Category: Lue W]]
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[[Category: Alpha-helical inner membrane protein]]
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[[Category: Schwarzer N]]
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[[Category: Cytoplasmic membrane]]
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[[Category: Ion channel]]
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[[Category: Transport protein]]
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Current revision

FNT family ion channel

PDB ID 4fc4

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