View source for 4iu9


==Crystal structure of a membrane transporter==
<StructureSection load='4iu9' size='340' side='right'caption='[[4iu9]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4iu9]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4IU9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4IU9 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.005&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4iu9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4iu9 OCA], [https://pdbe.org/4iu9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4iu9 RCSB], [https://www.ebi.ac.uk/pdbsum/4iu9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4iu9 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/NARU_ECOLI NARU_ECOLI] Involved in excretion of nitrite produced by the dissimilatory reduction of nitrate.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The nitrate/nitrite transporters NarK and NarU play an important role in nitrogen homeostasis in bacteria and belong to the nitrate/nitrite porter family (NNP) of the major facilitator superfamily (MFS) fold. The structure and functional mechanism of NarK and NarU remain unknown. Here, we report the crystal structure of NarU at a resolution of 3.1 A and systematic biochemical characterization. The two molecules of NarU in an asymmetric unit exhibit two distinct conformational states: occluded and partially inward-open. The substrate molecule nitrate appears to be coordinated by four highly conserved, charged, or polar amino acids. Structural and biochemical analyses allowed the identification of key amino acids that are involved in substrate gating and transport. The observed conformational differences of NarU, together with unique sequence features of the NNP family transporters, suggest a transport mechanism that might deviate from the canonical rocker-switch model.

Structure and mechanism of a nitrate transporter.,Yan H, Huang W, Yan C, Gong X, Jiang S, Zhao Y, Wang J, Shi Y Cell Rep. 2013 Mar 28;3(3):716-23. doi: 10.1016/j.celrep.2013.03.007. Epub 2013, Mar 21. PMID:23523348<ref>PMID:23523348</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4iu9" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli K-12]]
[[Category: Large Structures]]
[[Category: Gong X]]
[[Category: Huang W]]
[[Category: Jiang S]]
[[Category: Shi Y]]
[[Category: Wang J]]
[[Category: Yan C]]
[[Category: Yan H]]
[[Category: Zhao Y]]