1zun
From Proteopedia
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- | {{Seed}} | ||
- | [[Image:1zun.png|left|200px]] | ||
- | < | + | ==Crystal Structure of a GTP-Regulated ATP Sulfurylase Heterodimer from Pseudomonas syringae== |
- | + | <StructureSection load='1zun' size='340' side='right'caption='[[1zun]], [[Resolution|resolution]] 2.70Å' scene=''> | |
- | You may | + | == Structural highlights == |
- | + | <table><tr><td colspan='2'>[[1zun]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_syringae Pseudomonas syringae] and [https://en.wikipedia.org/wiki/Pseudomonas_syringae_pv._tomato_str._DC3000 Pseudomonas syringae pv. tomato str. DC3000]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZUN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZUN FirstGlance]. <br> | |
- | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7Å</td></tr> | |
- | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AGS:PHOSPHOTHIOPHOSPHORIC+ACID-ADENYLATE+ESTER'>AGS</scene>, <scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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=1zun FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zun OCA], [https://pdbe.org/1zun PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zun RCSB], [https://www.ebi.ac.uk/pdbsum/1zun PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zun ProSAT]</span></td></tr> | |
+ | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/CYSD_PSESM CYSD_PSESM] | ||
+ | == Evolutionary Conservation == | ||
+ | [[Image:Consurf_key_small.gif|200px|right]] | ||
+ | Check<jmol> | ||
+ | <jmolCheckbox> | ||
+ | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/zu/1zun_consurf.spt"</scriptWhenChecked> | ||
+ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
+ | <text>to colour the structure by Evolutionary Conservation</text> | ||
+ | </jmolCheckbox> | ||
+ | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1zun ConSurf]. | ||
+ | <div style="clear:both"></div> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | Sulfate assimilation is a critical component of both primary and secondary metabolism. An essential step in this pathway is the activation of sulfate through adenylation by the enzyme ATP sulfurylase (ATPS), forming adenosine 5'-phosphosulfate (APS). Proteobacterial ATPS overcomes this energetically unfavorable reaction by associating with a regulatory G protein, coupling the energy of GTP hydrolysis to APS formation. To discover the molecular basis of this unusual role for a G protein, we biochemically characterized and solved the X-ray crystal structure of a complex between Pseudomonas syringae ATPS (CysD) and its associated regulatory G protein (CysN). The structure of CysN*D shows the two proteins in tight association; however, the nucleotides bound to each subunit are spatially segregated. We provide evidence that conserved switch motifs in the G domain of CysN allosterically mediate interactions between the nucleotide binding sites. This structure suggests a molecular mechanism by which conserved G domain architecture is used to energetically link GTP turnover to the production of an essential metabolite. | ||
- | + | Molecular basis for G protein control of the prokaryotic ATP sulfurylase.,Mougous JD, Lee DH, Hubbard SC, Schelle MW, Vocadlo DJ, Berger JM, Bertozzi CR Mol Cell. 2006 Jan 6;21(1):109-22. PMID:16387658<ref>PMID:16387658</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
- | + | <div class="pdbe-citations 1zun" style="background-color:#fffaf0;"></div> | |
- | + | == References == | |
- | + | <references/> | |
- | + | __TOC__ | |
- | + | </StructureSection> | |
- | == | + | [[Category: Large Structures]] |
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- | == | + | |
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- | [[Category: | + | |
[[Category: Pseudomonas syringae]] | [[Category: Pseudomonas syringae]] | ||
- | [[Category: Pseudomonas syringae pv. tomato str. | + | [[Category: Pseudomonas syringae pv. tomato str. DC3000]] |
- | + | [[Category: Berger JM]] | |
- | [[Category: Berger | + | [[Category: Bertozzi CR]] |
- | [[Category: Bertozzi | + | [[Category: Hubbard SC]] |
- | [[Category: Hubbard | + | [[Category: Lee DH]] |
- | [[Category: Lee | + | [[Category: Mougous JD]] |
- | [[Category: Mougous | + | [[Category: Schelle MW]] |
- | [[Category: Schelle | + | [[Category: Vocadlo DJ]] |
- | [[Category: Vocadlo | + | |
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Current revision
Crystal Structure of a GTP-Regulated ATP Sulfurylase Heterodimer from Pseudomonas syringae
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