1l5h
From Proteopedia
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(New page: 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" | ||
- | caption="1l5h, resolution 2.3Å" /> | ||
- | '''FeMo-cofactor Deficient Nitrogenase MoFe Protein'''<br /> | ||
- | == | + | ==FeMo-cofactor Deficient Nitrogenase MoFe Protein== |
- | One of the most complex biosynthetic processes in metallobiochemistry is | + | <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> | |
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- | + | 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> | |
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- | + | ==See Also== | |
+ | *[[Nitrogenase 3D structures|Nitrogenase 3D structures]] | ||
+ | == References == | ||
+ | <references/> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Azotobacter vinelandii]] | ||
+ | [[Category: Large Structures]] | ||
+ | [[Category: Burgess BK]] | ||
+ | [[Category: Dean DR]] | ||
+ | [[Category: Einsle O]] | ||
+ | [[Category: Rees DC]] | ||
+ | [[Category: Ribbe MW]] | ||
+ | [[Category: Schmid B]] | ||
+ | [[Category: Thomas LM]] | ||
+ | [[Category: Yoshida M]] |
Current revision
FeMo-cofactor Deficient Nitrogenase MoFe Protein
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Categories: Azotobacter vinelandii | Large Structures | Burgess BK | Dean DR | Einsle O | Rees DC | Ribbe MW | Schmid B | Thomas LM | Yoshida M