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| - | {{Large structure}}
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| | ==Nitrogenase molybdenum-iron protein beta-K400E mutant== | | ==Nitrogenase molybdenum-iron protein beta-K400E mutant== |
| - | <StructureSection load='5cx1' size='340' side='right' caption='[[5cx1]], [[Resolution|resolution]] 1.75Å' scene=''> | + | <StructureSection load='5cx1' size='340' side='right'caption='[[5cx1]], [[Resolution|resolution]] 1.75Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5cx1]] is a 16 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_478 Atcc 478] and [http://en.wikipedia.org/wiki/Azotobacter_vinelandii Azotobacter vinelandii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CX1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5CX1 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5cx1]] is a 16 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=5CX1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5CX1 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CLF:FE(8)-S(7)+CLUSTER'>CLF</scene>, <scene name='pdbligand=HCA:3-HYDROXY-3-CARBOXY-ADIPIC+ACID'>HCA</scene>, <scene name='pdbligand=ICS:IRON-SULFUR-MOLYBDENUM+CLUSTER+WITH+INTERSTITIAL+CARBON'>ICS</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]] 1.7476Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1m1n|1m1n]], [[3u7q|3u7q]], [[2afh|2afh]], [[4wzb|4wzb]], [[2afi|2afi]], [[4wza|4wza]], [[1m34|1m34]]</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>, <scene name='pdbligand=HCA:3-HYDROXY-3-CARBOXY-ADIPIC+ACID'>HCA</scene>, <scene name='pdbligand=ICS:IRON-SULFUR-MOLYBDENUM+CLUSTER+WITH+INTERSTITIAL+CARBON'>ICS</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'>[https://proteopedia.org/fgij/fg.htm?mol=5cx1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cx1 OCA], [https://pdbe.org/5cx1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5cx1 RCSB], [https://www.ebi.ac.uk/pdbsum/5cx1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5cx1 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=5cx1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cx1 OCA], [http://pdbe.org/5cx1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5cx1 RCSB], [http://www.ebi.ac.uk/pdbsum/5cx1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5cx1 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| - | {{Large structure}} | |
| | == Function == | | == Function == |
| - | [[http://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. [[http://www.uniprot.org/uniprot/NIFK_AZOVI NIFK_AZOVI]] This molybdenum-iron protein is part of the nitrogenase complex that catalyzes the key enzymatic reactions in nitrogen fixation. | + | [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. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | ==See Also== | | ==See Also== |
| - | *[[Nitrogenase|Nitrogenase]] | + | *[[Nitrogenase 3D structures|Nitrogenase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 478]] | |
| | [[Category: Azotobacter vinelandii]] | | [[Category: Azotobacter vinelandii]] |
| - | [[Category: Nitrogenase]] | + | [[Category: Large Structures]] |
| - | [[Category: Luca, M A]] | + | [[Category: Luca MA]] |
| - | [[Category: Owens, C P]] | + | [[Category: Owens CP]] |
| - | [[Category: Tezcan, F A]] | + | [[Category: Tezcan FA]] |
| - | [[Category: Nitrogen fixation]]
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| - | [[Category: Oxidoreductase]]
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| Structural highlights
Function
NIFD_AZOVI This molybdenum-iron protein is part of the nitrogenase complex that catalyzes the key enzymatic reactions in nitrogen fixation.
Publication Abstract from PubMed
Nitrogenase is the only enzyme that can convert atmospheric dinitrogen (N2) into biologically usable ammonia (NH3). To achieve this multielectron redox process, the nitrogenase component proteins, MoFe-protein (MoFeP) and Fe-protein (FeP), repeatedly associate and dissociate in an ATP-dependent manner, where one electron is transferred from FeP to MoFeP per association. Here, we provide experimental evidence that encounter complexes between FeP and MoFeP play a functional role in nitrogenase catalysis. The encounter complexes are stabilized by electrostatic interactions involving a positively charged patch on the beta-subunit of MoFeP. Three single mutations (betaAsn399Glu, betaLys400Glu, and betaArg401Glu) in this patch were generated in Azotobacter vinelandii MoFeP. All of the resulting variants displayed decreases in specific catalytic activity, with the betaK400E mutation showing the largest effect. As simulated by the Thorneley-Lowe kinetic scheme, this single mutation lowered the rate constant for FeP-MoFeP association 5-fold. We also found that the betaK400E mutation did not affect the coupling of ATP hydrolysis with electron transfer (ET) between FeP and MoFeP. These data suggest a mechanism where FeP initially forms encounter complexes on the MoFeP beta-subunit surface en route to the ATP-activated, ET-competent complex over the alphabeta-interface.
Evidence for Functionally Relevant Encounter Complexes in Nitrogenase Catalysis.,Owens CP, Katz FE, Carter CH, Luca MA, Tezcan FA J Am Chem Soc. 2015 Oct 7;137(39):12704-12. doi: 10.1021/jacs.5b08310. Epub 2015 , Sep 24. PMID:26360912[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Owens CP, Katz FE, Carter CH, Luca MA, Tezcan FA. Evidence for Functionally Relevant Encounter Complexes in Nitrogenase Catalysis. J Am Chem Soc. 2015 Oct 7;137(39):12704-12. doi: 10.1021/jacs.5b08310. Epub 2015 , Sep 24. PMID:26360912 doi:http://dx.doi.org/10.1021/jacs.5b08310
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