1zun: Difference between revisions
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New page: left|200px<br /><applet load="1zun" size="450" color="white" frame="true" align="right" spinBox="true" caption="1zun, resolution 2.70Å" /> '''Crystal Structure of... |
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== | ==Crystal Structure of a GTP-Regulated ATP Sulfurylase Heterodimer from Pseudomonas syringae== | ||
Sulfate assimilation is a critical component of both primary and secondary | <StructureSection load='1zun' size='340' side='right'caption='[[1zun]], [[Resolution|resolution]] 2.70Å' scene=''> | ||
== 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> | |||
[[Category: | <div class="pdbe-citations 1zun" style="background-color:#fffaf0;"></div> | ||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[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 | |||
