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4dnx

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<StructureSection load='4dnx' size='340' side='right'caption='[[4dnx]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
<StructureSection load='4dnx' size='340' side='right'caption='[[4dnx]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4dnx]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Allvd Allvd]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DNX OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=4DNX FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4dnx]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Allochromatium_vinosum_DSM_180 Allochromatium vinosum DSM 180]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DNX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4DNX FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Alvin_1118, sat ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=572477 ALLVD])</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</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/Sulfate_adenylyltransferase Sulfate adenylyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.4 2.7.7.4] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4dnx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dnx OCA], [https://pdbe.org/4dnx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4dnx RCSB], [https://www.ebi.ac.uk/pdbsum/4dnx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4dnx ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=4dnx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dnx OCA], [http://pdbe.org/4dnx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4dnx RCSB], [http://www.ebi.ac.uk/pdbsum/4dnx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4dnx ProSAT]</span></td></tr>
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</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/SAT_ALLVD SAT_ALLVD]
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ATP sulfurylase (ATPS) catalyzes a key reaction in the global sulfur cycle by reversibly converting inorganic sulfate (SO4 (2-)) with ATP to adenosine 5'-phosphosulfate (APS) and pyrophosphate (PPi). In this work we report on the sat encoded dissimilatory ATP sulfurylase from the sulfur-oxidizing purple sulfur bacterium Allochromatium vinosum. In this organism, the sat gene is located in one operon and co-transcribed with the aprMBA genes for membrane-bound APS reductase. Like APS reductase, Sat is dispensible for growth on reduced sulfur compounds due to the presence of an alternate, so far unidentified sulfite-oxidizing pathway in A. vinosum. Sulfate assimilation also proceeds independently of Sat by a separate pathway involving a cysDN-encoded assimilatory ATP sulfurylase. We produced the purple bacterial sat-encoded ATP sulfurylase as a recombinant protein in E. coli, determined crucial kinetic parameters and obtained a crystal structure in an open state with a ligand-free active site. By comparison with several known structures of the ATPS-APS complex in the closed state a scenario about substrate-induced conformational changes was worked out. Despite different kinetic properties ATPS involved in sulfur-oxidizing and sulfate-reducing processes are not distinguishable on a structural level presumably due to the interference between functional and evolutionary processes.
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Structural, biochemical and genetic characterization of dissimilatory ATP sulfurylase from Allochromatium vinosum.,Parey K, Demmer U, Warkentin E, Wynen A, Ermler U, Dahl C PLoS One. 2013 Sep 20;8(9):e74707. doi: 10.1371/journal.pone.0074707. eCollection, 2013. PMID:24073218<ref>PMID:24073218</ref>
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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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<div class="pdbe-citations 4dnx" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Allvd]]
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[[Category: Allochromatium vinosum DSM 180]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Sulfate adenylyltransferase]]
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[[Category: Dahl C]]
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[[Category: Dahl, C]]
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[[Category: Demmer U]]
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[[Category: Demmer, U]]
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[[Category: Ermler U]]
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[[Category: Ermler, U]]
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[[Category: Parey K]]
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[[Category: Parey, K]]
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[[Category: Warkentin E]]
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[[Category: Warkentin, E]]
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[[Category: Adenylsulfurylase/atp:sulfate adenylyltransferase]]
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[[Category: Atp and ap]]
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[[Category: Respectively]]
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[[Category: Rossmann-like fold]]
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[[Category: Transferase]]
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Current revision

The structure of the ATP sulfurylase from Allochromatium vinosum in the open state

PDB ID 4dnx

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