4dnx

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (14:40, 14 March 2024) (edit) (undo)
 
Line 4: Line 4:
== Structural highlights ==
== Structural highlights ==
<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>
<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>
-
</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>
+
</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>
 +
<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>
<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>
<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>
</table>
</table>
== Function ==
== Function ==
-
[[https://www.uniprot.org/uniprot/SAT_ALLVD SAT_ALLVD]]
+
[https://www.uniprot.org/uniprot/SAT_ALLVD SAT_ALLVD]
-
<div style="background-color:#fffaf0;">
+
-
== Publication Abstract from PubMed ==
+
-
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.
+
-
 
+
-
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>
+
-
 
+
-
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+
-
</div>
+
-
<div class="pdbe-citations 4dnx" style="background-color:#fffaf0;"></div>
+
-
== References ==
+
-
<references/>
+
__TOC__
__TOC__
</StructureSection>
</StructureSection>

Current revision

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

PDB ID 4dnx

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4dnx"
Personal tools