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| | ==Crystal structure of yeast PAPS reductase with PAP, a product complex== | | ==Crystal structure of yeast PAPS reductase with PAP, a product complex== |
| - | <StructureSection load='2oq2' size='340' side='right' caption='[[2oq2]], [[Resolution|resolution]] 2.10Å' scene=''> | + | <StructureSection load='2oq2' size='340' side='right'caption='[[2oq2]], [[Resolution|resolution]] 2.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2oq2]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OQ2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2OQ2 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2oq2]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OQ2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2OQ2 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=A3P:ADENOSINE-3-5-DIPHOSPHATE'>A3P</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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MET16 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=A3P:ADENOSINE-3-5-DIPHOSPHATE'>A3P</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphoadenylyl-sulfate_reductase_(thioredoxin) Phosphoadenylyl-sulfate reductase (thioredoxin)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.4.8 1.8.4.8] </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=2oq2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2oq2 OCA], [https://pdbe.org/2oq2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2oq2 RCSB], [https://www.ebi.ac.uk/pdbsum/2oq2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2oq2 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=2oq2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2oq2 OCA], [http://pdbe.org/2oq2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2oq2 RCSB], [http://www.ebi.ac.uk/pdbsum/2oq2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2oq2 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/MET16_YEAST MET16_YEAST]] The NADP dependent reduction of PAPS into sulfite involves thioredoxin which probably plays the role of a thiol carrier. | + | [https://www.uniprot.org/uniprot/MET16_YEAST MET16_YEAST] The NADP dependent reduction of PAPS into sulfite involves thioredoxin which probably plays the role of a thiol carrier. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| | Check<jmol> | | Check<jmol> |
| | <jmolCheckbox> | | <jmolCheckbox> |
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/oq/2oq2_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/oq/2oq2_consurf.spt"</scriptWhenChecked> |
| | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 18824]] | + | [[Category: Large Structures]] |
| - | [[Category: Fisher, A J]] | + | [[Category: Saccharomyces cerevisiae]] |
| - | [[Category: Yu, Z]] | + | [[Category: Fisher AJ]] |
| - | [[Category: Oxidoreductase]] | + | [[Category: Yu Z]] |
| - | [[Category: Paps reductase]]
| + | |
| - | [[Category: Sulfate reduction]]
| + | |
| Structural highlights
Function
MET16_YEAST The NADP dependent reduction of PAPS into sulfite involves thioredoxin which probably plays the role of a thiol carrier.
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
Most assimilatory bacteria, fungi, and plants species reduce sulfate (in the activated form of APS or PAPS) to produce reduced sulfur. In yeast, PAPS reductase reduces PAPS to sulfite and PAP. Despite the difference in substrate specificity and catalytic cofactor, PAPS reductase is homologous to APS reductase in both sequence and structure, and they are suggested to share the same catalytic mechanism. Metazoans do not possess the sulfate reduction pathway, which makes APS/PAPS reductases potential drug targets for human pathogens. Here, we present the 2.05 A resolution crystal structure of the yeast PAPS reductase binary complex with product PAP bound. The N-terminal region mediates dimeric interactions resulting in a unique homodimer assembly not seen in previous APS/PAPS reductase structures. The "pyrophosphate-binding" sequence (47)TTAFGLTG(54) defines the substrate 3'-phosphate binding pocket. In yeast, Gly54 replaces a conserved aspartate found in APS reductases vacating space and charge to accommodate the 3'-phosphate of PAPS, thus regulating substrate specificity. Also, for the first time, the complete C-terminal catalytic motif (244)ECGIH(248) is revealed in the active site. The catalytic residue Cys245 is ideally positioned for an in-line attack on the beta-sulfate of PAPS. In addition, the side chain of His248 is only 4.2 A from the Sgamma of Cys245 and may serve as a catalytic base to deprotonate the active site cysteine. A hydrophobic sequence (252)RFAQFL(257) at the end of the C-terminus may provide anchoring interactions preventing the tail from swinging away from the active site as seen in other APS/PAPS reductases.
Crystal structure of Saccharomyces cerevisiae 3'-phosphoadenosine-5'-phosphosulfate reductase complexed with adenosine 3',5'-bisphosphate.,Yu Z, Lemongello D, Segel IH, Fisher AJ Biochemistry. 2008 Dec 2;47(48):12777-86. PMID:18991405[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Yu Z, Lemongello D, Segel IH, Fisher AJ. Crystal structure of Saccharomyces cerevisiae 3'-phosphoadenosine-5'-phosphosulfate reductase complexed with adenosine 3',5'-bisphosphate. Biochemistry. 2008 Dec 2;47(48):12777-86. PMID:18991405 doi:10.1021/bi801118f
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