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| | <StructureSection load='1zun' size='340' side='right'caption='[[1zun]], [[Resolution|resolution]] 2.70Å' scene=''> | | <StructureSection load='1zun' size='340' side='right'caption='[[1zun]], [[Resolution|resolution]] 2.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1zun]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_19310 Atcc 19310] and [https://en.wikipedia.org/wiki/Psesm Psesm]. 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> | + | <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='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=NA:SODIUM+ION'>NA</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]] 2.7Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cysD ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=317 ATCC 19310]), cysNC ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=223283 PSESM])</td></tr>
| + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Sulfate_adenylyltransferase Sulfate adenylyltransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.4 2.7.7.4] </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=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> | | <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> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/CYSD_PSESM CYSD_PSESM] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 19310]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Psesm]] | + | [[Category: Pseudomonas syringae]] |
| - | [[Category: Sulfate adenylyltransferase]] | + | [[Category: Pseudomonas syringae pv. tomato str. DC3000]] |
| - | [[Category: Berger, J M]] | + | [[Category: Berger JM]] |
| - | [[Category: Bertozzi, C R]] | + | [[Category: Bertozzi CR]] |
| - | [[Category: Hubbard, S C]] | + | [[Category: Hubbard SC]] |
| - | [[Category: Lee, D H]] | + | [[Category: Lee DH]] |
| - | [[Category: Mougous, J D]] | + | [[Category: Mougous JD]] |
| - | [[Category: Schelle, M W]] | + | [[Category: Schelle MW]] |
| - | [[Category: Vocadlo, D J]] | + | [[Category: Vocadlo DJ]] |
| - | [[Category: Beta barrel]]
| + | |
| - | [[Category: G protein]]
| + | |
| - | [[Category: Gtpase]]
| + | |
| - | [[Category: Heterodimer]]
| + | |
| - | [[Category: Pyrophosphate]]
| + | |
| - | [[Category: Switch domain]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
1zun is a 2 chain structure with sequence from Pseudomonas syringae and Pseudomonas syringae pv. tomato str. DC3000. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 2.7Å |
| Ligands: | , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
CYSD_PSESM
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Mougous JD, Lee DH, Hubbard SC, Schelle MW, Vocadlo DJ, Berger JM, Bertozzi CR. Molecular basis for G protein control of the prokaryotic ATP sulfurylase. Mol Cell. 2006 Jan 6;21(1):109-22. PMID:16387658 doi:10.1016/j.molcel.2005.10.034
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