5frt: Difference between revisions

Revision as of 13:20, 26 July 2023

Structure of the FeSII (shethna) protein of Azotobacter vinelandii

Structural highlights

5frt is a 5 chain structure with sequence from Azotobacter vinelandii. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.34Å
Ligands:	FES
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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]

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:https://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

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OCA

[1] 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

[2] 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:https://dx.doi.org/10.1021/jacs.5b10341

[3] 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

[4] 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

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[2]

[3]

[4]

@@ Line 3: / Line 3: @@
 <StructureSection load='5frt' size='340' side='right'caption='[[5frt]], [[Resolution|resolution]] 2.34&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5frt]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_478 Atcc 478]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FRT OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5FRT FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5frt]] 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=5FRT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5FRT 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]] 2.34&#8491;</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=5frt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5frt OCA], [http://pdbe.org/5frt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5frt RCSB], [http://www.ebi.ac.uk/pdbsum/5frt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5frt 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=5frt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5frt OCA], [https://pdbe.org/5frt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5frt RCSB], [https://www.ebi.ac.uk/pdbsum/5frt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5frt ProSAT]</span></td></tr>
 </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>
+== References ==
+<references/>
 __TOC__
 </StructureSection>
-[[Category: Atcc 478]]
+[[Category: Azotobacter vinelandii]]
 [[Category: Large Structures]]
-[[Category: Cotton, C A.R]]
+[[Category: Cotton CAR]]
-[[Category: Kabasakal, B V]]
+[[Category: Kabasakal BV]]
-[[Category: Lieber, L]]
+[[Category: Lieber L]]
-[[Category: Murray, J W]]
+[[Category: Murray JW]]
-[[Category: Ferredoxin]]
-[[Category: Nitrogenase]]
-[[Category: Oxidoreductase]]
-[[Category: Oxygen protection]]

5frt: Difference between revisions

Revision as of 13:20, 26 July 2023

Structure of the FeSII (shethna) protein of Azotobacter vinelandii

Structural highlights

Function

References

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