|
|
| (3 intermediate revisions not shown.) |
| Line 1: |
Line 1: |
| | | | |
| | ==ArsC complexed with MNB== | | ==ArsC complexed with MNB== |
| - | <StructureSection load='1rxe' size='340' side='right' caption='[[1rxe]], [[Resolution|resolution]] 1.70Å' scene=''> | + | <StructureSection load='1rxe' size='340' side='right'caption='[[1rxe]], [[Resolution|resolution]] 1.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1rxe]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"micrococcus_aureus"_(rosenbach_1884)_zopf_1885 "micrococcus aureus" (rosenbach 1884) zopf 1885]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RXE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1RXE FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1rxe]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RXE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RXE FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=LCP:PERCHLORATE+ION'>LCP</scene>, <scene name='pdbligand=MNB:5-MERCAPTO-2-NITRO-BENZOIC+ACID'>MNB</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]] 1.7Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ljl|1ljl]], [[1rxi|1rxi]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=LCP:PERCHLORATE+ION'>LCP</scene>, <scene name='pdbligand=MNB:5-MERCAPTO-2-NITRO-BENZOIC+ACID'>MNB</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ARSC, SAP018 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1280 "Micrococcus aureus" (Rosenbach 1884) Zopf 1885])</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=1rxe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rxe OCA], [https://pdbe.org/1rxe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rxe RCSB], [https://www.ebi.ac.uk/pdbsum/1rxe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rxe 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/Arsenate_reductase_(glutaredoxin) Arsenate reductase (glutaredoxin)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.20.4.1 1.20.4.1] </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=1rxe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rxe OCA], [http://pdbe.org/1rxe PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1rxe RCSB], [http://www.ebi.ac.uk/pdbsum/1rxe PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1rxe ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/ARSC_STAAU ARSC_STAAU]] Reduces arsenate [As(V)] to arsenite [As(III)] and dephosphorylates tyrosine phosphorylated proteins, low-MW aryl phosphates and natural and synthetic acyl phosphates. Could switch between different functions in different circumstances.[HAMAP-Rule:MF_01624] | + | [https://www.uniprot.org/uniprot/ARSC_STAAU ARSC_STAAU] Reduces arsenate [As(V)] to arsenite [As(III)] and dephosphorylates tyrosine phosphorylated proteins, low-MW aryl phosphates and natural and synthetic acyl phosphates. Could switch between different functions in different circumstances.[HAMAP-Rule:MF_01624] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| Line 17: |
Line 15: |
| | <jmolCheckbox> | | <jmolCheckbox> |
| | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/rx/1rxe_consurf.spt"</scriptWhenChecked> | | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/rx/1rxe_consurf.spt"</scriptWhenChecked> |
| - | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
| | </jmolCheckbox> | | </jmolCheckbox> |
| Line 33: |
Line 31: |
| | | | |
| | ==See Also== | | ==See Also== |
| - | *[[Arsenate reductase|Arsenate reductase]] | + | *[[Arsenate reductase 3D structures|Arsenate reductase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Belle, K Van]] | + | [[Category: Large Structures]] |
| - | [[Category: Limbourg, M]] | + | [[Category: Staphylococcus aureus]] |
| - | [[Category: Loris, R]] | + | [[Category: Limbourg M]] |
| - | [[Category: Martins, J C]] | + | [[Category: Loris R]] |
| - | [[Category: Messens, J]] | + | [[Category: Martins JC]] |
| - | [[Category: Molle, I Van]] | + | [[Category: Messens J]] |
| - | [[Category: Vanhaesebrouck, P]]
| + | [[Category: Van Belle K]] |
| - | [[Category: Wahni, K]]
| + | [[Category: Van Molle I]] |
| - | [[Category: Wyns, L]] | + | [[Category: Vanhaesebrouck P]] |
| - | [[Category: 5-mercapto-2-nitrobenzoic acid]] | + | [[Category: Wahni K]] |
| - | [[Category: 5-thio-2-nitrobenzoic acid]] | + | [[Category: Wyns L]] |
| - | [[Category: Arsc]] | + | |
| - | [[Category: Mixed disulphide]]
| + | |
| - | [[Category: Mnb]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Tnb]]
| + | |
| Structural highlights
Function
ARSC_STAAU Reduces arsenate [As(V)] to arsenite [As(III)] and dephosphorylates tyrosine phosphorylated proteins, low-MW aryl phosphates and natural and synthetic acyl phosphates. Could switch between different functions in different circumstances.[HAMAP-Rule:MF_01624]
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
Structural insights into formation of the complex between the ubiquitous thiol-disulfide oxidoreductase thioredoxin and its oxidized substrate are under-documented owing to its entropical instability. In vitro, it is possible via a reaction with 5,5'-dithiobis-(2-nitrobenzoic acid) to make a stable mixed-disulfide complex between thioredoxin from Staphylococcus aureus and one of its substrates, oxidized pI258 arsenate reductase (ArsC) from S. aureus. In the absence of the crystal structure of an ArsC-thioredoxin complex, the structures of two precursors of the complex, the ArsC triple mutant ArsC C10SC15AC82S and its 5-thio-2-nitrobenzoic acid (TNB) adduct, were determined. The ArsC triple mutant has a structure very similar to that of the reduced form of wild-type ArsC, with a folded redox helix and a buried catalytic Cys89. In the adduct form, the TNB molecule is buried in a hydrophobic pocket and the disulfide bridge between TNB and Cys89 is sterically inaccessible to thioredoxin. In order to form a mixed disulfide between ArsC and thioredoxin, a change in the orientation of the TNB-Cys89 disulfide in the structure is necessary.
The structure of a triple mutant of pI258 arsenate reductase from Staphylococcus aureus and its 5-thio-2-nitrobenzoic acid adduct.,Messens J, Van Molle I, Vanhaesebrouck P, Van Belle K, Wahni K, Martins JC, Wyns L, Loris R Acta Crystallogr D Biol Crystallogr. 2004 Jun;60(Pt 6):1180-4. Epub 2004, May 21. PMID:15159594[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Messens J, Van Molle I, Vanhaesebrouck P, Van Belle K, Wahni K, Martins JC, Wyns L, Loris R. The structure of a triple mutant of pI258 arsenate reductase from Staphylococcus aureus and its 5-thio-2-nitrobenzoic acid adduct. Acta Crystallogr D Biol Crystallogr. 2004 Jun;60(Pt 6):1180-4. Epub 2004, May 21. PMID:15159594 doi:10.1107/S0907444904007334
|
