5cb8

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'''Unreleased structure'''
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==Crystal structure of Adenosine-5'-phosphosulfate kinase in complex with APS and sulfate==
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<StructureSection load='5cb8' size='340' side='right' caption='[[5cb8]], [[Resolution|resolution]] 1.88&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5cb8]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CB8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5CB8 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=ADX:ADENOSINE-5-PHOSPHOSULFATE'>ADX</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<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>
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<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=5cb8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cb8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=5cb8 RCSB], [http://www.ebi.ac.uk/pdbsum/5cb8 PDBsum]</span></td></tr>
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</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/CYSC_SYNY3 CYSC_SYNY3]] Catalyzes the synthesis of activated sulfate.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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The entry 5cb8 is ON HOLD until Paper Publication
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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<ref>PMID:26294763</ref>
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Authors: Herrmann, J., Jez, J.M.
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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Description: Crystal structure of Adenosine-5'-phosphosulfate kinase in complex with APS and sulfate
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== References ==
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[[Category: Unreleased Structures]]
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Adenylyl-sulfate kinase]]
[[Category: Herrmann, J]]
[[Category: Herrmann, J]]
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[[Category: Jez, J.M]]
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[[Category: Jez, J M]]
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[[Category: Kinase]]
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[[Category: Sulfur metabolism]]
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[[Category: Synechocysti]]
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[[Category: Transferase]]

Revision as of 12:26, 2 September 2015

Crystal structure of Adenosine-5'-phosphosulfate kinase in complex with APS and sulfate

5cb8, resolution 1.88Å

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