6rk0
From Proteopedia
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<StructureSection load='6rk0' size='340' side='right'caption='[[6rk0]], [[Resolution|resolution]] 0.99Å' scene=''> | <StructureSection load='6rk0' size='340' side='right'caption='[[6rk0]], [[Resolution|resolution]] 0.99Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[6rk0]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6RK0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6RK0 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6rk0]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Azovd Azovd]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6RK0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6RK0 FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Avin_49040 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=322710 AZOVD])</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=6rk0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rk0 OCA], [http://pdbe.org/6rk0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6rk0 RCSB], [http://www.ebi.ac.uk/pdbsum/6rk0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6rk0 ProSAT]</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=6rk0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rk0 OCA], [http://pdbe.org/6rk0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6rk0 RCSB], [http://www.ebi.ac.uk/pdbsum/6rk0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6rk0 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The biological route for nitrogen gas entering the biosphere is reduction to ammonia by the nitrogenase enzyme, which is inactivated by oxygen. Three types of nitrogenase exist, the least studied of which is the iron-only nitrogenase. The Anf3 protein in the bacterium Rhodobacter capsulatus is essential for diazotrophic (i.e. nitrogen-fixing) growth with the iron-only nitrogenase, but its enzymatic activity and function are unknown. Here, we biochemically and structurally characterize Anf3 from the model diazotrophic bacterium Azotobacter vinelandii. Determining the Anf3 crystal structure to atomic resolution, we observed that it is a dimeric flavocytochrome with an unusually close interaction between the heme and the flavin adenine dinucleotide cofactors. Measuring the reduction potentials by spectroelectrochemical redox titration, we observed values of -420 +/- 10 mV and -330 +/- 10 mV for the two FAD potentials and -340 +/- 1 mV for the heme. We further show that Anf3 accepts electrons from spinach ferredoxin and that Anf3 consumes oxygen without generating superoxide or hydrogen peroxide. We predict that Anf3 protects the iron-only nitrogenase from oxygen inactivation by functioning as an oxidase in respiratory protection, with flavodoxin or ferredoxin as the physiological electron donors. | ||
| + | |||
| + | A low-potential terminal oxidase associated with the iron-only nitrogenase from the nitrogen-fixing bacterium Azotobacter vinelandii.,Varghese F, Kabasakal BV, Cotton CA, Schumacher J, Rutherford AW, Fantuzzi A, Murray JW J Biol Chem. 2019 May 1. pii: RA118.007285. doi: 10.1074/jbc.RA118.007285. PMID:31043481<ref>PMID:31043481</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6rk0" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Azovd]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Kabasakal, B]] | [[Category: Kabasakal, B]] | ||
Revision as of 08:24, 21 May 2019
Structure of the Flavocytochrome Anf3 from Azotobacter vinelandii
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