1zun
From Proteopedia
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|PDB= 1zun |SIZE=350|CAPTION= <scene name='initialview01'>1zun</scene>, resolution 2.70Å | |PDB= 1zun |SIZE=350|CAPTION= <scene name='initialview01'>1zun</scene>, resolution 2.70Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <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> |
| - | |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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|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]) | |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]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1zun FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zun OCA], [http://www.ebi.ac.uk/pdbsum/1zun PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1zun RCSB]</span> | ||
}} | }} | ||
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[[Category: Schelle, M W.]] | [[Category: Schelle, M W.]] | ||
[[Category: Vocadlo, D J.]] | [[Category: Vocadlo, D J.]] | ||
| - | [[Category: AGS]] | ||
| - | [[Category: GDP]] | ||
| - | [[Category: MG]] | ||
| - | [[Category: NA]] | ||
[[Category: beta barrel]] | [[Category: beta barrel]] | ||
[[Category: g protein]] | [[Category: g protein]] | ||
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[[Category: switch domain]] | [[Category: switch domain]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:41:49 2008'' |
Revision as of 22:41, 30 March 2008
| |||||||
| , resolution 2.70Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , , | ||||||
| Gene: | cysD (Pseudomonas syringae), cysNC (Pseudomonas syringae pv. tomato str. DC3000) | ||||||
| Activity: | Sulfate adenylyltransferase, with EC number 2.7.7.4 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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 Mon Mar 31 01:41:49 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. | Beta barrel | G protein | Gtpase | Heterodimer | Pyrophosphate | Switch domain
