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| | <StructureSection load='5koh' size='340' side='right'caption='[[5koh]], [[Resolution|resolution]] 1.83Å' scene=''> | | <StructureSection load='5koh' size='340' side='right'caption='[[5koh]], [[Resolution|resolution]] 1.83Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5koh]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Gluda Gluda]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KOH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5KOH FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5koh]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Gluconacetobacter_diazotrophicus_PA1_5 Gluconacetobacter diazotrophicus PA1 5]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KOH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5KOH FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CLF:FE(8)-S(7)+CLUSTER'>CLF</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</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>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=MRD:(4R)-2-METHYLPENTANE-2,4-DIOL'>MRD</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]] 1.83Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3u7q|3u7q]], [[2min|2min]], [[3min|3min]], [[1qgu|1qgu]], [[1qh1|1qh1]], [[4wes|4wes]], [[5koj|5koj]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CLF:FE(8)-S(7)+CLUSTER'>CLF</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</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>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=MRD:(4R)-2-METHYLPENTANE-2,4-DIOL'>MRD</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=5koh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5koh OCA], [https://pdbe.org/5koh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5koh RCSB], [https://www.ebi.ac.uk/pdbsum/5koh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5koh 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=5koh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5koh OCA], [http://pdbe.org/5koh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5koh RCSB], [http://www.ebi.ac.uk/pdbsum/5koh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5koh ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/A9H5W5_GLUDA A9H5W5_GLUDA] |
| | <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: Gluda]] | + | [[Category: Gluconacetobacter diazotrophicus PA1 5]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Nitrogenase]]
| + | [[Category: Owens CP]] |
| - | [[Category: Owens, C P]] | + | [[Category: Tezcan FA]] |
| - | [[Category: Tezcan, F A]] | + | |
| - | [[Category: Electron transfer]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: P-cluster]]
| + | |
| Structural highlights
5koh is a 4 chain structure with sequence from Gluconacetobacter diazotrophicus PA1 5. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 1.83Å |
| Ligands: | , , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
A9H5W5_GLUDA
Publication Abstract from PubMed
The P-cluster is a unique iron-sulfur center that likely functions as a dynamic electron (e(-)) relay site between the Fe-protein and the catalytic FeMo-cofactor in nitrogenase. The P-cluster has been shown to undergo large conformational changes upon 2-e(-) oxidation which entail the coordination of two of the Fe centers to a Ser side chain and a backbone amide N, respectively. Yet, how and if this 2-e(-) oxidized state (P(OX)) is involved in catalysis by nitrogenase is not well established. Here, we present the crystal structures of reduced and oxidized MoFe-protein (MoFeP) from Gluconacetobacter diazotrophicus (Gd), which natively possesses an Ala residue in the position of the Ser ligand to the P-cluster. While reduced Gd-MoFeP is structurally identical to previously characterized counterparts around the FeMo-cofactor, oxidized Gd-MoFeP features an unusual Tyr coordination to its P-cluster along with ligation by a backbone amide nitrogen. EPR analysis of the oxidized Gd-MoFeP P-cluster confirmed that it is a 2-e(-) oxidized, integer-spin species. Importantly, we have found that the sequence positions corresponding to the Ser and Tyr ligands are almost completely covariant among Group I nitrogenases. These findings strongly support the possibility that the P(OX) state is functionally relevant in nitrogenase catalysis and that a hard, O-based anionic ligand serves to stabilize this state in a switchable fashion.
Tyrosine-Coordinated P-Cluster in G. diazotrophicus Nitrogenase: Evidence for the Importance of O-Based Ligands in Conformationally Gated Electron Transfer.,Owens CP, Katz FE, Carter CH, Oswald VF, Tezcan FA J Am Chem Soc. 2016 Aug 17;138(32):10124-7. doi: 10.1021/jacs.6b06783. Epub 2016 , Aug 8. PMID:27487256[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Owens CP, Katz FE, Carter CH, Oswald VF, Tezcan FA. Tyrosine-Coordinated P-Cluster in G. diazotrophicus Nitrogenase: Evidence for the Importance of O-Based Ligands in Conformationally Gated Electron Transfer. J Am Chem Soc. 2016 Aug 17;138(32):10124-7. doi: 10.1021/jacs.6b06783. Epub 2016 , Aug 8. PMID:27487256 doi:http://dx.doi.org/10.1021/jacs.6b06783
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