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[[Image:1n2c.jpg|left|200px]]


{{Structure
==NITROGENASE COMPLEX FROM AZOTOBACTER VINELANDII STABILIZED BY ADP-TETRAFLUOROALUMINATE==
|PDB= 1n2c |SIZE=350|CAPTION= <scene name='initialview01'>1n2c</scene>, resolution 3.0&Aring;
<StructureSection load='1n2c' size='340' side='right'caption='[[1n2c]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ALF:TETRAFLUOROALUMINATE+ION'>ALF</scene>, <scene name='pdbligand=HCA:3-HYDROXY-3-CARBOXY-ADIPIC+ACID'>HCA</scene>, <scene name='pdbligand=CFM:FE-MO-S+CLUSTER'>CFM</scene>, <scene name='pdbligand=CLF:FE(8)-S(7)+CLUSTER'>CLF</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene> and <scene name='pdbligand=ADP:ADENOSINE-5&#39;-DIPHOSPHATE'>ADP</scene>
<table><tr><td colspan='2'>[[1n2c]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Azotobacter_vinelandii Azotobacter vinelandii]. The February 2002 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Nitrogenase''  by David S. Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2002_2 10.2210/rcsb_pdb/mom_2002_2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N2C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1N2C FirstGlance]. <br>
|ACTIVITY= [http://en.wikipedia.org/wiki/Nitrogenase Nitrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.18.6.1 1.18.6.1]
</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&#8491;</td></tr>
|GENE=
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=ALF:TETRAFLUOROALUMINATE+ION'>ALF</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=HCA:3-HYDROXY-3-CARBOXY-ADIPIC+ACID'>HCA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=1n2c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n2c OCA], [https://pdbe.org/1n2c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1n2c RCSB], [https://www.ebi.ac.uk/pdbsum/1n2c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1n2c ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/NIFD_AZOVI NIFD_AZOVI] This molybdenum-iron protein is part of the nitrogenase complex that catalyzes the key enzymatic reactions in nitrogen fixation.
== 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/n2/1n2c_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=1n2c ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The coupling of ATP hydrolysis to electron transfer by the enzyme nitrogenase during biological nitrogen fixation is an important example of a nucleotide-dependent transduction mechanism. The crystal structure has been determined for the complex between the Fe-protein and MoFe-protein components of nitrogenase stabilized by ADP x AIF4-, previously used as a nucleoside triphosphate analogue in nucleotide-switch proteins. The structure reveals that the dimeric Fe-protein has undergone substantial conformational changes. The beta-phosphate and AIF4- groups are stabilized through intersubunit contacts that are critical for catalysis and the redox centre is repositioned to facilitate electron transfer. Interactions in the nitrogenase complex have broad implications for signal and energy transduction mechanisms in multiprotein complexes.


'''NITROGENASE COMPLEX FROM AZOTOBACTER VINELANDII STABILIZED BY ADP-TETRAFLUOROALUMINATE'''
Structure of ADP x AIF4(-)-stabilized nitrogenase complex and its implications for signal transduction.,Schindelin H, Kisker C, Schlessman JL, Howard JB, Rees DC Nature. 1997 May 22;387(6631):370-6. PMID:9163420<ref>PMID:9163420</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1n2c" style="background-color:#fffaf0;"></div>


==Overview==
==See Also==
The coupling of ATP hydrolysis to electron transfer by the enzyme nitrogenase during biological nitrogen fixation is an important example of a nucleotide-dependent transduction mechanism. The crystal structure has been determined for the complex between the Fe-protein and MoFe-protein components of nitrogenase stabilized by ADP x AIF4-, previously used as a nucleoside triphosphate analogue in nucleotide-switch proteins. The structure reveals that the dimeric Fe-protein has undergone substantial conformational changes. The beta-phosphate and AIF4- groups are stabilized through intersubunit contacts that are critical for catalysis and the redox centre is repositioned to facilitate electron transfer. Interactions in the nitrogenase complex have broad implications for signal and energy transduction mechanisms in multiprotein complexes.
*[[Nitrogenase|Nitrogenase]]
 
*[[Nitrogenase 3D structures|Nitrogenase 3D structures]]
==About this Structure==
== References ==
1N2C is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Azotobacter_vinelandii Azotobacter vinelandii]. The following page contains interesting information on the relation of 1N2C with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb26_1.html Nitrogenase]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N2C OCA].
<references/>
 
__TOC__
==Reference==
</StructureSection>
Structure of ADP x AIF4(-)-stabilized nitrogenase complex and its implications for signal transduction., Schindelin H, Kisker C, Schlessman JL, Howard JB, Rees DC, Nature. 1997 May 22;387(6631):370-6. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9163420 9163420]
[[Category: Azotobacter vinelandii]]
[[Category: Azotobacter vinelandii]]
[[Category: Large Structures]]
[[Category: Nitrogenase]]
[[Category: Nitrogenase]]
[[Category: Protein complex]]
[[Category: RCSB PDB Molecule of the Month]]
[[Category: Kisker, C.]]
[[Category: Kisker C]]
[[Category: Rees, D C.]]
[[Category: Rees DC]]
[[Category: Schindelin, H.]]
[[Category: Schindelin H]]
[[Category: ADP]]
[[Category: ALF]]
[[Category: CA]]
[[Category: CFM]]
[[Category: CLF]]
[[Category: HCA]]
[[Category: MG]]
[[Category: SF4]]
[[Category: atp hydrolysis]]
[[Category: complex of nitrogenase protein]]
[[Category: electron transfer]]
[[Category: nitrogen fixation]]
[[Category: nitrogenase]]
[[Category: signal transduction]]
 
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Retrieved from "https://proteopedia.org/1n2c"