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1zun
From Proteopedia
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| - | [[Image:1zun.gif|left|200px]] | + | [[Image:1zun.gif|left|200px]] |
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| - | '''Crystal Structure of a GTP-Regulated ATP Sulfurylase Heterodimer from Pseudomonas syringae''' | + | {{Structure |
| + | |PDB= 1zun |SIZE=350|CAPTION= <scene name='initialview01'>1zun</scene>, resolution 2.70Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=GDP:GUANOSINE-5'-DIPHOSPHATE'>GDP</scene> and <scene name='pdbligand=AGS:PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER'>AGS</scene> | ||
| + | |ACTIVITY= [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] | ||
| + | |GENE= cysD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=317 Pseudomonas syringae]), cysNC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=223283 Pseudomonas syringae pv. tomato str. DC3000]) | ||
| + | }} | ||
| + | |||
| + | '''Crystal Structure of a GTP-Regulated ATP Sulfurylase Heterodimer from Pseudomonas syringae''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1ZUN is a [ | + | 1ZUN is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Pseudomonas_syringae Pseudomonas syringae] and [http://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]. |
==Reference== | ==Reference== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/16387658 16387658] |
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Pseudomonas syringae]] | [[Category: Pseudomonas syringae]] | ||
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[[Category: switch domain]] | [[Category: switch domain]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:40:01 2008'' |
Revision as of 13:40, 20 March 2008
| |||||||
| , resolution 2.70Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , and | ||||||
| Gene: | cysD (Pseudomonas syringae), cysNC (Pseudomonas syringae pv. tomato str. DC3000) | ||||||
| Activity: | Sulfate adenylyltransferase, with EC number 2.7.7.4 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure of a GTP-Regulated ATP Sulfurylase Heterodimer from Pseudomonas syringae
Overview
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.
About this Structure
1ZUN is a Protein complex structure of sequences from Pseudomonas syringae and Pseudomonas syringae pv. tomato str. dc3000. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Mar 20 15:40:01 2008
Categories: Protein complex | Pseudomonas syringae | Pseudomonas syringae pv. tomato str. dc3000 | Sulfate adenylyltransferase | Berger, J M. | Bertozzi, C R. | Hubbard, S C. | Lee, D H. | Mougous, J D. | Schelle, M W. | Vocadlo, D J. | AGS | GDP | MG | NA | Beta barrel | G protein | Gtpase | Heterodimer | Pyrophosphate | Switch domain
