6q93
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==MgADP-bound Fe protein of Vanadium nitrogenase from Azotobacter vinelandii== | |
| + | <StructureSection load='6q93' size='340' side='right' caption='[[6q93]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6q93]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Azotobacter_vinelandii_(strain_dj_/_atcc_baa-1303) Azotobacter vinelandii (strain dj / atcc baa-1303)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6Q93 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6Q93 FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6q93 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6q93 OCA], [http://pdbe.org/6q93 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6q93 RCSB], [http://www.ebi.ac.uk/pdbsum/6q93 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6q93 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/C1DI30_AZOVD C1DI30_AZOVD]] The key enzymatic reactions in nitrogen fixation are catalyzed by the nitrogenase complex, which has 2 components: the iron protein and the molybdenum-iron protein.[HAMAP-Rule:MF_00533] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Nitrogenases catalyze the biological fixation of inert N2 into bioavailable ammonium. They are bipartite systems consisting of the catalytic dinitrogenase and a complementary reductase, the Fe protein that is also the site where ATP is hydrolyzed to drive the reaction forward. Three different subclasses of dinitrogenases are known, employing either molybdenum, vanadium or only iron at their active site cofactor. Although in all these classes the mode and mechanism of interaction with Fe protein is conserved, each one encodes its own orthologue of the reductase in the corresponding gene cluster. Here we present the 2.2 A resolution structure of VnfH from Azotobacter vinelandii, the Fe protein of the alternative, vanadium-dependent nitrogenase system, in its ADP-bound state. VnfH adopts the same conformation that was observed for NifH, the Fe protein of molybdenum nitrogenase, in complex with ADP, representing a state of the functional cycle that is ready for reduction and subsequent nucleotide exchange. The overall similarity of NifH and VnfH confirms the experimentally determined cross-reactivity of both ATP-hydrolyzing reductases. | ||
| - | + | Crystal structure of VnfH, the iron protein component of vanadium nitrogenase.,Rohde M, Trncik C, Sippel D, Gerhardt S, Einsle O J Biol Inorg Chem. 2018 Oct;23(7):1049-1056. doi: 10.1007/s00775-018-1602-4. Epub, 2018 Aug 23. PMID:30141094<ref>PMID:30141094</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 6q93" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Nitrogenase]] | ||
| + | [[Category: Einsle, O]] | ||
[[Category: Gerhardt, S]] | [[Category: Gerhardt, S]] | ||
[[Category: Rohde, M]] | [[Category: Rohde, M]] | ||
| - | [[Category: | + | [[Category: Biological nitrogen fixation]] |
| + | [[Category: Dinitrogenase reductase]] | ||
| + | [[Category: Electron transport]] | ||
| + | [[Category: Fe protein]] | ||
| + | [[Category: Vanadium nitrogenase]] | ||
| + | [[Category: Vnfh]] | ||
Revision as of 15:34, 27 February 2019
MgADP-bound Fe protein of Vanadium nitrogenase from Azotobacter vinelandii
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