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| | <StructureSection load='5cb6' size='340' side='right'caption='[[5cb6]], [[Resolution|resolution]] 2.79Å' scene=''> | | <StructureSection load='5cb6' size='340' side='right'caption='[[5cb6]], [[Resolution|resolution]] 2.79Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5cb6]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Syny3 Syny3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CB6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5CB6 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5cb6]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Synechocystis_sp._PCC_6803_substr._Kazusa Synechocystis sp. PCC 6803 substr. Kazusa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CB6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5CB6 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADX:ADENOSINE-5-PHOSPHOSULFATE'>ADX</scene>, <scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=CAC:CACODYLATE+ION'>CAC</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADX:ADENOSINE-5-PHOSPHOSULFATE'>ADX</scene>, <scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=CAC:CACODYLATE+ION'>CAC</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cysC, slr0676 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1111708 SYNY3])</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=5cb6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cb6 OCA], [https://pdbe.org/5cb6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5cb6 RCSB], [https://www.ebi.ac.uk/pdbsum/5cb6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5cb6 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/Adenylyl-sulfate_kinase Adenylyl-sulfate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.25 2.7.1.25] </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=5cb6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cb6 OCA], [http://pdbe.org/5cb6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5cb6 RCSB], [http://www.ebi.ac.uk/pdbsum/5cb6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5cb6 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CYSC_SYNY3 CYSC_SYNY3]] Catalyzes the synthesis of activated sulfate. | + | [https://www.uniprot.org/uniprot/CYSC_SYNY3 CYSC_SYNY3] Catalyzes the synthesis of activated sulfate. |
| | <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: Adenylyl-sulfate kinase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Syny3]] | + | [[Category: Synechocystis sp. PCC 6803 substr. Kazusa]] |
| - | [[Category: Herrmann, J]] | + | [[Category: Herrmann J]] |
| - | [[Category: Jez, J M]] | + | [[Category: Jez JM]] |
| - | [[Category: Enzyme]]
| + | |
| - | [[Category: Kinase]]
| + | |
| - | [[Category: Sulfur metabolism]]
| + | |
| - | [[Category: Synechocysti]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
CYSC_SYNY3 Catalyzes the synthesis of activated sulfate.
Publication Abstract from PubMed
In plants, adenosine 5'-phosphosulfate (APS) kinase (APSK) is required for reproductive viability and the production of 3'-phosphoadenosine-5'-phosphosulfate (PAPS) as a sulfur-donor in specialized metabolism. Previous studies of the APSK from Arabidopsis thaliana (AtAPSK) identified a regulatory disulfide bond formed between the N-terminal domain (NTD) and a cysteine on the core scaffold. This thiol-switch is unique to mosses, gymnosperms, and angiosperms. To understand the structural evolution of redox-control of APSK, we investigated the redox-insensitive APSK from the cyanobacterium Synechocystis sp. PCC 6803 (SynAPSK). Crystallographic analysis of SynAPSK in complex with either APS and a non-hydrolyzable ATP analog or APS and sulfate reveals the overall structure of the enzyme, which lacks the NTD found in homologs from mosses and plants. A series of engineered SynAPSK variants reconstruct the structural evolution of the plant APSK. Biochemical analyses of SynAPSK, SynAPSK H23C mutant, SynAPSK fused to the AtAPSK NTD, and the fusion protein with the H23C mutation show that addition of the NTD and cysteines recapitulates thiol-based regulation. These results reveal the molecular basis for structural changes leading to the evolution of redox-control in APSK of the green lineage from cyanobacteria to plants.
Recapitulating the Structural Evolution of Redox-Regulation in Adenosine-5'-Phosphosulfate Kinase from Cyanobacteria to Plants.,Herrmann J, Nathin D, Lee SG, Sun T, Jez JM J Biol Chem. 2015 Aug 20. pii: jbc.M115.679514. PMID:26294763[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Herrmann J, Nathin D, Lee SG, Sun T, Jez JM. Recapitulating the Structural Evolution of Redox-Regulation in Adenosine-5'-Phosphosulfate Kinase from Cyanobacteria to Plants. J Biol Chem. 2015 Aug 20. pii: jbc.M115.679514. PMID:26294763 doi:http://dx.doi.org/10.1074/jbc.M115.679514
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