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==FeMo-cofactor Deficient Nitrogenase MoFe Protein== | |||
<StructureSection load='1l5h' size='340' side='right'caption='[[1l5h]], [[Resolution|resolution]] 2.30Å' 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]] 2.3Å</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>, <scene name='pdbligand=CLF:FE(8)-S(7)+CLUSTER'>CLF</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/initialview01.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. | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</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: | [[Category: Large Structures]] | ||
[[Category: Burgess BK]] | |||
[[Category: Burgess | [[Category: Dean DR]] | ||
[[Category: Dean | [[Category: Einsle O]] | ||
[[Category: Einsle | [[Category: Rees DC]] | ||
[[Category: Rees | [[Category: Ribbe MW]] | ||
[[Category: Ribbe | [[Category: Schmid B]] | ||
[[Category: Schmid | [[Category: Thomas LM]] | ||
[[Category: Thomas | [[Category: Yoshida M]] | ||
[[Category: Yoshida | |||
Latest revision as of 12:09, 16 August 2023
FeMo-cofactor Deficient Nitrogenase MoFe ProteinFeMo-cofactor Deficient Nitrogenase MoFe Protein
Structural highlights
FunctionNIFD_AZOVI This molybdenum-iron protein is part of the nitrogenase complex that catalyzes the key enzymatic reactions in nitrogen fixation. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedOne 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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