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| | <StructureSection load='5ffi' size='340' side='right'caption='[[5ffi]], [[Resolution|resolution]] 2.17Å' scene=''> | | <StructureSection load='5ffi' size='340' side='right'caption='[[5ffi]], [[Resolution|resolution]] 2.17Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5ffi]] is a 5 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FFI OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5FFI FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5ffi]] is a 5 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=5FFI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5FFI FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.17Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5ffi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ffi OCA], [http://pdbe.org/5ffi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ffi RCSB], [http://www.ebi.ac.uk/pdbsum/5ffi PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ffi ProSAT]</span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</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=5ffi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ffi OCA], [https://pdbe.org/5ffi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ffi RCSB], [https://www.ebi.ac.uk/pdbsum/5ffi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ffi ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/FESII_AZOVI FESII_AZOVI] Binds to and protects nitrogenase from irreversible exposure to O(2), in what is known as 'conformational protection' (PubMed:7830548, PubMed:7548055, PubMed:10220344, PubMed:26654855). Shifts nitrogenase into an inactive, O(2)-tolerant state. Exists in 2 states, an open oxidized state that binds and protects nitrogenase, and a closed reduced state that probably does not bind nitrogenase; cooperative oxidation of the 2Fe-2S clusters causes the conformation change (PubMed:26654855). Does not protect nitrogenase with the vanadium-iron subunit, not clear if it protects the iron-only nitrogenase (PubMed:7830548).<ref>PMID:10220344</ref> <ref>PMID:26654855</ref> <ref>PMID:7548055</ref> <ref>PMID:7830548</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | + | [[Category: Azotobacter vinelandii]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Einsle, O]] | + | [[Category: Einsle O]] |
| - | [[Category: Gerhardt, S]] | + | [[Category: Gerhardt S]] |
| - | [[Category: Rohde, M]] | + | [[Category: Rohde M]] |
| - | [[Category: Schlesier, J]] | + | [[Category: Schlesier J]] |
| - | [[Category: Ferredoxin]]
| + | |
| - | [[Category: Fesii]]
| + | |
| - | [[Category: Metal binding protein]]
| + | |
| - | [[Category: Nitrogen fixation]]
| + | |
| - | [[Category: Nitrogenase]]
| + | |
| - | [[Category: Shethna protein ii]]
| + | |
| Structural highlights
Function
FESII_AZOVI Binds to and protects nitrogenase from irreversible exposure to O(2), in what is known as 'conformational protection' (PubMed:7830548, PubMed:7548055, PubMed:10220344, PubMed:26654855). Shifts nitrogenase into an inactive, O(2)-tolerant state. Exists in 2 states, an open oxidized state that binds and protects nitrogenase, and a closed reduced state that probably does not bind nitrogenase; cooperative oxidation of the 2Fe-2S clusters causes the conformation change (PubMed:26654855). Does not protect nitrogenase with the vanadium-iron subunit, not clear if it protects the iron-only nitrogenase (PubMed:7830548).[1] [2] [3] [4]
Publication Abstract from PubMed
The two-component metalloprotein nitrogenase catalyzes the reductive fixation of atmospheric dinitrogen into bioavailable ammonium in diazotrophic prokaryotes. The process requires an efficient energy metabolism, so that although the metal clusters of nitrogenase rapidly decompose in the presence of dioxygen, many free-living diazotrophs are obligate aerobes. In order to retain the functionality of the nitrogen-fixing enzyme, some of these are able to rapidly "switch-off" nitrogenase, by shifting the enzyme into an inactive but oxygen-tolerant state. Under these conditions the two components of nitrogenase form a stable, ternary complex with a small [2Fe:2S] ferredoxin termed FeSII or the "Shethna protein II". Here we have produced and isolated Azotobacter vinelandii FeS II and have determined its three-dimensional structure to 2.1 A resolution by X-ray diffraction. In the crystals, the dimeric protein was present in two distinct states that differ in the conformation of an extended loop in close proximity to the iron-sulfur cluster. We show that this rearrangement is redox-dependent and forms the molecular basis for oxygen-dependent conformational protection of nitrogenase. Protection assays highlight that FeSII binds to a preformed complex of MoFe and Fe protein upon activation, primarily through electrostatic interactions. The surface properties and known complexes of nitrogenase component proteins allow us to propose a model of the conformationally protected ternary complex of nitrogenase.
A Conformational Switch Triggers Nitrogenase Protection from Oxygen Damage by Shethna Protein II (FeSII).,Schlesier J, Rohde M, Gerhardt S, Einsle O J Am Chem Soc. 2015 Dec 24. PMID:26654855[5]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Lou J, Moshiri F, Johnson MK, Lafferty ME, Sorkin DL, Miller A, Maier RJ. Mutagenesis studies of the FeSII protein of Azotobacter vinelandii: roles of histidine and lysine residues in the protection of nitrogenase from oxygen damage. Biochemistry. 1999 Apr 27;38(17):5563-71. PMID:10220344 doi:10.1021/bi9827823
- ↑ Schlesier J, Rohde M, Gerhardt S, Einsle O. A Conformational Switch Triggers Nitrogenase Protection from Oxygen Damage by Shethna Protein II (FeSII). J Am Chem Soc. 2015 Dec 24. PMID:26654855 doi:http://dx.doi.org/10.1021/jacs.5b10341
- ↑ Moshiri F, Crouse BR, Johnson MK, Maier RJ. The "nitrogenase-protective" FeSII protein of Azotobacter vinelandii: overexpression, characterization, and crystallization. Biochemistry. 1995 Oct 10;34(40):12973-82. PMID:7548055 doi:10.1021/bi00040a007
- ↑ Moshiri F, Kim JW, Fu C, Maier RJ. The FeSII protein of Azotobacter vinelandii is not essential for aerobic nitrogen fixation, but confers significant protection to oxygen-mediated inactivation of nitrogenase in vitro and in vivo. Mol Microbiol. 1994 Oct;14(1):101-14. PMID:7830548 doi:10.1111/j.1365-2958.1994.tb01270.x
- ↑ Schlesier J, Rohde M, Gerhardt S, Einsle O. A Conformational Switch Triggers Nitrogenase Protection from Oxygen Damage by Shethna Protein II (FeSII). J Am Chem Soc. 2015 Dec 24. PMID:26654855 doi:http://dx.doi.org/10.1021/jacs.5b10341
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