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New page: left|200px<br /><applet load="1l5h" size="450" color="white" frame="true" align="right" spinBox="true" caption="1l5h, resolution 2.3Å" /> '''FeMo-cofactor Deficie...
 
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[[Image:1l5h.jpg|left|200px]]<br /><applet load="1l5h" size="450" color="white" frame="true" align="right" spinBox="true"
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'''FeMo-cofactor Deficient Nitrogenase MoFe Protein'''<br />


==Overview==
==FeMo-cofactor Deficient Nitrogenase MoFe Protein==
One of the most complex biosynthetic processes in metallobiochemistry is, the assembly of nitrogenase, the key enzyme in biological nitrogen, fixation. We describe here the crystal structure of an iron-molybdenum, cofactor-deficient form of the nitrogenase MoFe protein, into which the, cofactor is inserted in the final step of MoFe protein assembly. The MoFe, protein folds as a heterotetramer containing two copies each of the, homologous alpha and beta subunits. In this structure, one of the three, alpha subunit domains exhibits a substantially changed conformation, whereas the rest of the protein remains essentially unchanged. A, predominantly positively charged funnel is revealed; this funnel is of, sufficient size to accommodate insertion of the negatively charged, cofactor.
<StructureSection load='1l5h' size='340' side='right'caption='[[1l5h]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1l5h]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Azotobacter_vinelandii Azotobacter vinelandii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L5H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1L5H 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]] 2.3&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</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=1l5h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l5h OCA], [https://pdbe.org/1l5h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1l5h RCSB], [https://www.ebi.ac.uk/pdbsum/1l5h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1l5h 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/l5/1l5h_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=1l5h ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
One of the most complex biosynthetic processes in metallobiochemistry is the assembly of nitrogenase, the key enzyme in biological nitrogen fixation. We describe here the crystal structure of an iron-molybdenum cofactor-deficient form of the nitrogenase MoFe protein, into which the cofactor is inserted in the final step of MoFe protein assembly. The MoFe protein folds as a heterotetramer containing two copies each of the homologous alpha and beta subunits. In this structure, one of the three alpha subunit domains exhibits a substantially changed conformation, whereas the rest of the protein remains essentially unchanged. A predominantly positively charged funnel is revealed; this funnel is of sufficient size to accommodate insertion of the negatively charged cofactor.


==About this Structure==
Structure of a cofactor-deficient nitrogenase MoFe protein.,Schmid B, Ribbe MW, Einsle O, Yoshida M, Thomas LM, Dean DR, Rees DC, Burgess BK Science. 2002 Apr 12;296(5566):352-6. PMID:11951047<ref>PMID:11951047</ref>
1L5H is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Azotobacter_vinelandii Azotobacter vinelandii] with CA and CLF as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1L5H OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Structure of a cofactor-deficient nitrogenase MoFe protein., Schmid B, Ribbe MW, Einsle O, Yoshida M, Thomas LM, Dean DR, Rees DC, Burgess BK, Science. 2002 Apr 12;296(5566):352-6. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11951047 11951047]
</div>
<div class="pdbe-citations 1l5h" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Nitrogenase 3D structures|Nitrogenase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Azotobacter vinelandii]]
[[Category: Azotobacter vinelandii]]
[[Category: Nitrogenase]]
[[Category: Large Structures]]
[[Category: Protein complex]]
[[Category: Burgess BK]]
[[Category: Burgess, B.K.]]
[[Category: Dean DR]]
[[Category: Dean, D.R.]]
[[Category: Einsle O]]
[[Category: Einsle, O.]]
[[Category: Rees DC]]
[[Category: Rees, D.C.]]
[[Category: Ribbe MW]]
[[Category: Ribbe, M.W.]]
[[Category: Schmid B]]
[[Category: Schmid, B.]]
[[Category: Thomas LM]]
[[Category: Thomas, L.M.]]
[[Category: Yoshida M]]
[[Category: Yoshida, M.]]
[[Category: CA]]
[[Category: CLF]]
[[Category: apo-protein]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 20:16:52 2007''

Latest revision as of 06:27, 13 August 2026

FeMo-cofactor Deficient Nitrogenase MoFe Protein

1l5h, resolution 2.30Å

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