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New page: left|200px<br /><applet load="1r27" size="450" color="white" frame="true" align="right" spinBox="true" caption="1r27, resolution 2.00Å" /> '''Crystal Structure of...
 
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[[Image:1r27.gif|left|200px]]<br /><applet load="1r27" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1r27, resolution 2.00&Aring;" />
'''Crystal Structure of NarGH complex'''<br />


==Overview==
==Crystal Structure of NarGH complex==
The structure of the catalytic and electron-transfer subunits (NarGH) of, the integral membrane protein, respiratory nitrate reductase (Nar) has, been determined to 2.0 A resolution revealing the molecular architecture, of this Mo-bisMGD (molybdopterin-guanine-dinucleotide) containing enzyme, which includes a previously undetected FeS cluster. Nar, together with the, related enzyme formate dehydrogenase (Fdh-N), is a key enzyme in the, generation of proton motive force across the membrane in Escherichia coli, nitrate respiration. A comparative study revealed that Nar and Fdh-N, employ different approaches for acquiring substrate, reflecting different, catalytic mechanisms. Nar uses a very narrow and nonpolar, substrate-conducting cavity with a nonspecific substrate binding site, whereas Fdh-N accommodates a wider, positively charged, substrate-conducting cavity with a more specific substrate binding site., The Nar structure also demonstrates the first example of an Asp side chain, acting as a Mo ligand providing a structural basis for the classification, of Mo-bisMGD enzymes.
<StructureSection load='1r27' size='340' side='right'caption='[[1r27]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1r27]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R27 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1R27 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]] 2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MGD:2-AMINO-5,6-DIMERCAPTO-7-METHYL-3,7,8A,9-TETRAHYDRO-8-OXA-1,3,9,10-TETRAAZA-ANTHRACEN-4-ONE+GUANOSINE+DINUCLEOTIDE'>MGD</scene>, <scene name='pdbligand=MO:MOLYBDENUM+ATOM'>MO</scene></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=1r27 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r27 OCA], [https://pdbe.org/1r27 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1r27 RCSB], [https://www.ebi.ac.uk/pdbsum/1r27 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1r27 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/NARG_ECOLI NARG_ECOLI] The nitrate reductase enzyme complex allows E.coli to use nitrate as an electron acceptor during anaerobic growth. The alpha chain is the actual site of nitrate reduction.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/r2/1r27_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1r27 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The structure of the catalytic and electron-transfer subunits (NarGH) of the integral membrane protein, respiratory nitrate reductase (Nar) has been determined to 2.0 A resolution revealing the molecular architecture of this Mo-bisMGD (molybdopterin-guanine-dinucleotide) containing enzyme which includes a previously undetected FeS cluster. Nar, together with the related enzyme formate dehydrogenase (Fdh-N), is a key enzyme in the generation of proton motive force across the membrane in Escherichia coli nitrate respiration. A comparative study revealed that Nar and Fdh-N employ different approaches for acquiring substrate, reflecting different catalytic mechanisms. Nar uses a very narrow and nonpolar substrate-conducting cavity with a nonspecific substrate binding site, whereas Fdh-N accommodates a wider, positively charged substrate-conducting cavity with a more specific substrate binding site. The Nar structure also demonstrates the first example of an Asp side chain acting as a Mo ligand providing a structural basis for the classification of Mo-bisMGD enzymes.


==About this Structure==
Architecture of NarGH reveals a structural classification of Mo-bisMGD enzymes.,Jormakka M, Richardson D, Byrne B, Iwata S Structure. 2004 Jan;12(1):95-104. PMID:14725769<ref>PMID:14725769</ref>
1R27 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with MO, F3S, SF4 and MGD as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Nitrate_reductase Nitrate reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.7.99.4 1.7.99.4] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1R27 OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Architecture of NarGH reveals a structural classification of Mo-bisMGD enzymes., Jormakka M, Richardson D, Byrne B, Iwata S, Structure. 2004 Jan;12(1):95-104. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=14725769 14725769]
</div>
<div class="pdbe-citations 1r27" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Nitrate reductase|Nitrate reductase]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Nitrate reductase]]
[[Category: Large Structures]]
[[Category: Protein complex]]
[[Category: Byrne B]]
[[Category: Byrne, B.]]
[[Category: Iwata S]]
[[Category: Iwata, S.]]
[[Category: Jormakka M]]
[[Category: Jormakka, M.]]
[[Category: Richardson D]]
[[Category: Richardson, D.]]
[[Category: F3S]]
[[Category: MGD]]
[[Category: MO]]
[[Category: SF4]]
[[Category: beta barrel; x-ray crystallography]]
 
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Retrieved from "https://proteopedia.org/1r27"