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| | ==Sulfurtransferase from Azotobacter vinelandii in complex with phosphate== | | ==Sulfurtransferase from Azotobacter vinelandii in complex with phosphate== |
| - | <StructureSection load='1h4m' size='340' side='right' caption='[[1h4m]], [[Resolution|resolution]] 2.10Å' scene=''> | + | <StructureSection load='1h4m' size='340' side='right'caption='[[1h4m]], [[Resolution|resolution]] 2.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1h4m]] is a 1 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=1H4M OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1H4M FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1h4m]] is a 1 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=1H4M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1H4M FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</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]] 2.1Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1e0c|1e0c]], [[1h4k|1h4k]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RHDA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=354 ATCC 478])</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=1h4m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h4m OCA], [https://pdbe.org/1h4m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1h4m RCSB], [https://www.ebi.ac.uk/pdbsum/1h4m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1h4m ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Thiosulfate_sulfurtransferase Thiosulfate sulfurtransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.8.1.1 2.8.1.1] </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=1h4m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h4m OCA], [http://pdbe.org/1h4m PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1h4m RCSB], [http://www.ebi.ac.uk/pdbsum/1h4m PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1h4m ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/THTR_AZOVI THTR_AZOVI] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </div> | | </div> |
| | <div class="pdbe-citations 1h4m" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 1h4m" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Sulfurtransferase|Sulfurtransferase]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 478]] | + | [[Category: Azotobacter vinelandii]] |
| - | [[Category: Thiosulfate sulfurtransferase]] | + | [[Category: Large Structures]] |
| - | [[Category: Bolognesi, M]] | + | [[Category: Bolognesi M]] |
| - | [[Category: Bordo, D]] | + | [[Category: Bordo D]] |
| - | [[Category: Carpen, A]] | + | [[Category: Carpen A]] |
| - | [[Category: Colnaghi, R]] | + | [[Category: Colnaghi R]] |
| - | [[Category: Forlani, F]] | + | [[Category: Forlani F]] |
| - | [[Category: Pagani, S]] | + | [[Category: Pagani S]] |
| - | [[Category: Spallarossa, A]] | + | [[Category: Spallarossa A]] |
| - | [[Category: Sulfur metabolism]]
| + | |
| - | [[Category: Thiosulfate:cyanide]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
THTR_AZOVI
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Active site reactivity and specificity of RhdA, a thiosulfate:cyanide sulfurtransferase (rhodanese) from Azotobacter vinelandii, have been investigated through ligand binding, site-directed mutagenesis, and X-ray crystallographic techniques, in a combined approach. In native RhdA the active site Cys230 is found persulfurated; fluorescence and sulfurtransferase activity measurements show that phosphate anions interact with Cys230 persulfide sulfur atom and modulate activity. Crystallographic analyses confirm that phosphate and hypophosphite anions react with native RhdA, removing the persulfide sulfur atom from the active site pocket. Considering that RhdA and the catalytic subunit of Cdc25 phosphatases share a common three-dimensional fold as well as active site Cys (catalytic) and Arg residues, two RhdA mutants carrying a single amino acid insertion at the active site loop were designed and their phosphatase activity tested. The crystallographic and functional results reported here show that specific sulfurtransferase or phosphatase activities are strictly related to precise tailoring of the catalytic loop structure in RhdA and Cdc25 phosphatase, respectively.
A persulfurated cysteine promotes active site reactivity in Azotobacter vinelandii Rhodanese.,Bordo D, Forlani F, Spallarossa A, Colnaghi R, Carpen A, Bolognesi M, Pagani S Biol Chem. 2001 Aug;382(8):1245-52. PMID:11592406[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Bordo D, Forlani F, Spallarossa A, Colnaghi R, Carpen A, Bolognesi M, Pagani S. A persulfurated cysteine promotes active site reactivity in Azotobacter vinelandii Rhodanese. Biol Chem. 2001 Aug;382(8):1245-52. PMID:11592406
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