This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1zun
From Proteopedia
| Line 4: | Line 4: | ||
|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> | ||
}} | }} | ||
| Line 31: | Line 34: | ||
[[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]] | ||
| Line 42: | Line 41: | ||
[[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
