1jzw: Difference between revisions
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==Arsenate Reductase + Sodium Arsenate From E. coli== | ==Arsenate Reductase + Sodium Arsenate From E. coli== | ||
<StructureSection load='1jzw' size='340' side='right' caption='[[1jzw]], [[Resolution|resolution]] 1.76Å' scene=''> | <StructureSection load='1jzw' size='340' side='right' caption='[[1jzw]], [[Resolution|resolution]] 1.76Å' scene=''> | ||
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSR:S-ARSONOCYSTEINE'>CSR</scene></td></tr> | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSR:S-ARSONOCYSTEINE'>CSR</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1i9d|1i9d]], [[1j9b|1j9b]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1i9d|1i9d]], [[1j9b|1j9b]]</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=1jzw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jzw OCA], [http://pdbe.org/1jzw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1jzw RCSB], [http://www.ebi.ac.uk/pdbsum/1jzw PDBsum]</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=1jzw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jzw OCA], [http://pdbe.org/1jzw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1jzw RCSB], [http://www.ebi.ac.uk/pdbsum/1jzw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1jzw ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/ | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1jzw ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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</div> | </div> | ||
<div class="pdbe-citations 1jzw" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 1jzw" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 10:12, 11 October 2017
Arsenate Reductase + Sodium Arsenate From E. coliArsenate Reductase + Sodium Arsenate From E. coli
Structural highlights
Function[ARSC1_ECOLX] Reduction of arsenate [As(V)] to arsenite [As(III)]. This protein expands the substrate specificity of ArsAB pump which can extrude arsenite and antimonite to allow for arsenate pumping and resistance. 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 PubMedBACKGROUND: In Escherichia coli bearing the plasmid R773, resistance to arsenite, arsenate, antimonite, and tellurite is conferred by the arsRDABC plasmid operon that codes for an ATP-dependent anion pump. The product of the arsC gene, arsenate reductase (ArsC), is required to efficiently catalyze the reduction of arsenate to arsenite prior to extrusion. RESULTS: Here, we report the first X-ray crystal structures of ArsC at 1.65 A and of ArsC complexed with arsenate and arsenite at 1.26 A resolution. The overall fold is unique. The native structure shows sulfate and sulfite ions binding in the active site as analogs of arsenate and arsenite. The covalent adduct of arsenate with Cys-12 in the active site of ArsC, which was analyzed in a difference map, shows tetrahedral geometry with a sulfur-arsenic distance of 2.18 A. However, the corresponding adduct with arsenite binds as a hitherto unseen thiarsahydroxy adduct. Finally, the number of bound waters (385) in this highly ordered crystal structure approaches twice the number expected at this resolution for a structure of 138 ordered residues. CONCLUSIONS: Structural information from the adduct of ArsC with its substrate (arsenate) and with its product (arsenite) together with functional information from mutational and biochemical studies on ArsC suggest a plausible mechanism for the reaction. The exceptionally well-defined water structure indicates that this crystal system has precise long-range order within the crystal and that the upper limit for the number of bound waters in crystal structures is underestimated by the structures in the Protein Data Bank. Insights into the structure, solvation, and mechanism of ArsC arsenate reductase, a novel arsenic detoxification enzyme.,Martin P, DeMel S, Shi J, Gladysheva T, Gatti DL, Rosen BP, Edwards BF Structure. 2001 Nov;9(11):1071-81. PMID:11709171[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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