1zun
From Proteopedia
(New page: 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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| - | [[Image:1zun.gif|left|200px]]<br /><applet load="1zun" size=" | + | [[Image:1zun.gif|left|200px]]<br /><applet load="1zun" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1zun, resolution 2.70Å" /> | caption="1zun, resolution 2.70Å" /> | ||
'''Crystal Structure of a GTP-Regulated ATP Sulfurylase Heterodimer from Pseudomonas syringae'''<br /> | '''Crystal Structure of a GTP-Regulated ATP Sulfurylase Heterodimer from Pseudomonas syringae'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Sulfate assimilation is a critical component of both primary and secondary | + | 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== | ==About this Structure== | ||
| - | 1ZUN is a [http://en.wikipedia.org/wiki/Protein_complex 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] with MG, NA, GDP and AGS as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http:// | + | 1ZUN is a [http://en.wikipedia.org/wiki/Protein_complex 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] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=NA:'>NA</scene>, <scene name='pdbligand=GDP:'>GDP</scene> and <scene name='pdbligand=AGS:'>AGS</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZUN OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Pseudomonas syringae pv. tomato str. dc3000]] | [[Category: Pseudomonas syringae pv. tomato str. dc3000]] | ||
[[Category: Sulfate adenylyltransferase]] | [[Category: Sulfate adenylyltransferase]] | ||
| - | [[Category: Berger, J | + | [[Category: Berger, J M.]] |
| - | [[Category: Bertozzi, C | + | [[Category: Bertozzi, C R.]] |
| - | [[Category: Hubbard, S | + | [[Category: Hubbard, S C.]] |
| - | [[Category: Lee, D | + | [[Category: Lee, D H.]] |
| - | [[Category: Mougous, J | + | [[Category: Mougous, J D.]] |
| - | [[Category: Schelle, M | + | [[Category: Schelle, M W.]] |
| - | [[Category: Vocadlo, D | + | [[Category: Vocadlo, D J.]] |
[[Category: AGS]] | [[Category: AGS]] | ||
[[Category: GDP]] | [[Category: GDP]] | ||
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[[Category: switch domain]] | [[Category: switch domain]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:19:13 2008'' |
Revision as of 14:19, 21 February 2008
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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 with , , and as ligands. Active as Sulfate adenylyltransferase, with EC number 2.7.7.4 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 Feb 21 16:19:13 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
