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| | ==Crystal Structure of the arsenite oxidase protein complex from Rhizobium species strain NT-26== | | ==Crystal Structure of the arsenite oxidase protein complex from Rhizobium species strain NT-26== |
| - | <StructureSection load='4aay' size='340' side='right' caption='[[4aay]], [[Resolution|resolution]] 2.70Å' scene=''> | + | <StructureSection load='4aay' size='340' side='right'caption='[[4aay]], [[Resolution|resolution]] 2.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4aay]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Arsenite-oxidising_bacterium_nt-26 Arsenite-oxidising bacterium nt-26]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AAY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4AAY FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4aay]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudorhizobium_banfieldiae Pseudorhizobium banfieldiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AAY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4AAY FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=4MO:MOLYBDENUM(IV)+ION'>4MO</scene>, <scene name='pdbligand=F3S:FE3-S4+CLUSTER'>F3S</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=MGD:2-AMINO-5,6-DIMERCAPTO-7-METHYL-3,7,8A,9-TETRAHYDRO-8-OXA-1,3,9,10-TETRAAZA-ANTHRACEN-4-ONE+GUANOSINE+DINUCLEOTIDE'>MGD</scene>, <scene name='pdbligand=O:OXYGEN+ATOM'>O</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]] 2.7Å</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=4aay FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4aay OCA], [http://pdbe.org/4aay PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4aay RCSB], [http://www.ebi.ac.uk/pdbsum/4aay PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4aay ProSAT]</span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=4MO:MOLYBDENUM(IV)+ION'>4MO</scene>, <scene name='pdbligand=F3S:FE3-S4+CLUSTER'>F3S</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=MGD:2-AMINO-5,6-DIMERCAPTO-7-METHYL-3,7,8A,9-TETRAHYDRO-8-OXA-1,3,9,10-TETRAAZA-ANTHRACEN-4-ONE+GUANOSINE+DINUCLEOTIDE'>MGD</scene>, <scene name='pdbligand=O:OXYGEN+ATOM'>O</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=4aay FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4aay OCA], [https://pdbe.org/4aay PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4aay RCSB], [https://www.ebi.ac.uk/pdbsum/4aay PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4aay ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q6VAL8_9HYPH Q6VAL8_9HYPH] |
| | <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: Arsenite-oxidising bacterium nt-26]] | + | [[Category: Large Structures]] |
| - | [[Category: Naismith, J H]] | + | [[Category: Pseudorhizobium banfieldiae]] |
| - | [[Category: Oke, M]] | + | [[Category: Naismith JH]] |
| - | [[Category: Santini, J M]] | + | [[Category: Oke M]] |
| - | [[Category: Iron sulfur]] | + | [[Category: Santini JM]] |
| - | [[Category: Molybdopterin]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Rieske]]
| + | |
| Structural highlights
4aay is a 8 chain structure with sequence from Pseudorhizobium banfieldiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 2.7Å |
| Ligands: | , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
Q6VAL8_9HYPH
Publication Abstract from PubMed
The arsenite oxidase (Aio) from the facultative autotrophic Alphaproteobacterium Rhizobium sp. NT-26 is a bioenergetic enzyme involved in the oxidation of arsenite to arsenate. The enzyme from the distantly related heterotroph, Alcaligenes faecalis, which is thought to oxidise arsenite for detoxification, consists of a large alpha subunit (AioA) with bis-molybdopterin guanine dinucleotide at its active site and a 3Fe-4S cluster, and a small beta subunit (AioB) which contains a Rieske 2Fe-2S cluster. The successful heterologous expression of the NT-26 Aio in Escherichia coli has resulted in the solution of its crystal structure. The NT-26 Aio, a heterotetramer, shares high overall similarity to the heterodimeric arsenite oxidase from A. faecalis but there are striking differences in the structure surrounding the Rieske 2Fe-2S cluster which we demonstrate explains the difference in the observed redox potentials (+225 mV vs. +130/160 mV, respectively). A combination of site-directed mutagenesis and electron paramagnetic resonance was used to explore the differences observed in the structure and redox properties of the Rieske cluster. In the NT-26 AioB the substitution of a serine (S126 in NT-26) for a threonine as in the A. faecalis AioB explains a -20 mV decrease in redox potential. The disulphide bridge in the A. faecalis AioB which is conserved in other betaproteobacterial AioB subunits and the Rieske subunit of the cytochrome bc 1 complex is absent in the NT-26 AioB subunit. The introduction of a disulphide bridge had no effect on Aio activity or protein stability but resulted in a decrease in the redox potential of the cluster. These results are in conflict with previous data on the betaproteobacterial AioB subunit and the Rieske of the bc 1 complex where removal of the disulphide bridge had no effect on the redox potential of the former but a decrease in cluster stability was observed in the latter.
The respiratory arsenite oxidase: structure and the role of residues surrounding the rieske cluster.,Warelow TP, Oke M, Schoepp-Cothenet B, Dahl JU, Bruselat N, Sivalingam GN, Leimkuhler S, Thalassinos K, Kappler U, Naismith JH, Santini JM PLoS One. 2013 Aug 30;8(8):e72535. doi: 10.1371/journal.pone.0072535. PMID:24023621[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Warelow TP, Oke M, Schoepp-Cothenet B, Dahl JU, Bruselat N, Sivalingam GN, Leimkuhler S, Thalassinos K, Kappler U, Naismith JH, Santini JM. The respiratory arsenite oxidase: structure and the role of residues surrounding the rieske cluster. PLoS One. 2013 Aug 30;8(8):e72535. doi: 10.1371/journal.pone.0072535. PMID:24023621 doi:10.1371/journal.pone.0072535
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