4u4t: Difference between revisions

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==Structure of a nitrate/nitrite antiporter NarK in nitrate-bound inward-open state==
==Structure of a nitrate/nitrite antiporter NarK in nitrate-bound inward-open state==
<StructureSection load='4u4t' size='340' side='right' caption='[[4u4t]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
<StructureSection load='4u4t' size='340' side='right' caption='[[4u4t]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene>, <scene name='pdbligand=OLA:OLEIC+ACID'>OLA</scene>, <scene name='pdbligand=OLC:(2R)-2,3-DIHYDROXYPROPYL+(9Z)-OCTADEC-9-ENOATE'>OLC</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene>, <scene name='pdbligand=OLA:OLEIC+ACID'>OLA</scene>, <scene name='pdbligand=OLC:(2R)-2,3-DIHYDROXYPROPYL+(9Z)-OCTADEC-9-ENOATE'>OLC</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4u4w|4u4w]], [[4u4v|4u4v]]</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4u4w|4u4w]], [[4u4v|4u4v]]</td></tr>
<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=4u4t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4u4t OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4u4t RCSB], [http://www.ebi.ac.uk/pdbsum/4u4t PDBsum]</span></td></tr>
<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=4u4t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4u4t OCA], [http://pdbe.org/4u4t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4u4t RCSB], [http://www.ebi.ac.uk/pdbsum/4u4t PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4u4t ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
<div class="pdbe-citations 4u4t" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>

Revision as of 16:23, 19 April 2017

Structure of a nitrate/nitrite antiporter NarK in nitrate-bound inward-open stateStructure of a nitrate/nitrite antiporter NarK in nitrate-bound inward-open state

Structural highlights

4u4t is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:, , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[NARK_ECOLI] Involved in excretion of nitrite produced by the dissimilatory reduction of nitrate.

Publication Abstract from PubMed

NarK belongs to the nitrate/nitrite porter (NNP) family in the major facilitator superfamily (MFS) and plays a central role in nitrate uptake across the membrane in diverse organisms, including archaea, bacteria, fungi and plants. Although previous studies provided insight into the overall structure and the substrate recognition of NarK, its molecular mechanism, including the driving force for nitrate transport, remained elusive. Here we demonstrate that NarK is a nitrate/nitrite antiporter, using an in vitro reconstituted system. Furthermore, we present the high-resolution crystal structures of NarK from Escherichia coli in the nitrate-bound occluded, nitrate-bound inward-open and apo inward-open states. The integrated structural, functional and computational analyses reveal the nitrate/nitrite antiport mechanism of NarK, in which substrate recognition is coupled to the transport cycle by the concomitant movement of the transmembrane helices and the key tyrosine and arginine residues in the substrate-binding site.

Structural basis for dynamic mechanism of nitrate/nitrite antiport by NarK.,Fukuda M, Takeda H, Kato HE, Doki S, Ito K, Maturana AD, Ishitani R, Nureki O Nat Commun. 2015 May 11;6:7097. doi: 10.1038/ncomms8097. PMID:25959928[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Fukuda M, Takeda H, Kato HE, Doki S, Ito K, Maturana AD, Ishitani R, Nureki O. Structural basis for dynamic mechanism of nitrate/nitrite antiport by NarK. Nat Commun. 2015 May 11;6:7097. doi: 10.1038/ncomms8097. PMID:25959928 doi:http://dx.doi.org/10.1038/ncomms8097

4u4t, resolution 2.40Å

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