1zun: Difference between revisions

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[[Image:1zun.gif|left|200px]]<br /><applet load="1zun" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1zun.gif|left|200px]]<br /><applet load="1zun" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1zun, resolution 2.70Å" />

'''Crystal Structure of a GTP-Regulated ATP Sulfurylase Heterodimer from Pseudomonas syringae'''<br />

==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.

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 [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://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1ZUN OCA].

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==

Line 15:

[[Category: Pseudomonas syringae pv. tomato str. dc3000]]

[[Category: Sulfate adenylyltransferase]]

[[Category: Berger, J.M.]]

[[Category: Berger, J M.]]

[[Category: Bertozzi, C.R.]]

[[Category: Bertozzi, C R.]]

[[Category: Hubbard, S.C.]]

[[Category: Hubbard, S C.]]

[[Category: Lee, D.H.]]

[[Category: Lee, D H.]]

[[Category: Mougous, J.D.]]

[[Category: Mougous, J D.]]

[[Category: Schelle, M.W.]]

[[Category: Schelle, M W.]]

[[Category: Vocadlo, D.J.]]

[[Category: Vocadlo, D J.]]

[[Category: AGS]]

[[Category: GDP]]

Line 33:

[[Category: switch domain]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:19:13 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1zun.gif|left|200px]]<br /><applet load="1zun" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1zun.gif|left|200px]]<br /><applet load="1zun" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1zun, resolution 2.70&Aring;" />
 '''Crystal Structure of a GTP-Regulated ATP Sulfurylase Heterodimer from Pseudomonas syringae'''<br />
 ==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.
+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==
-ZUN 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ZUN OCA].
+ZUN 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==
@@ Line 15: / Line 15: @@
 [[Category: Pseudomonas syringae pv. tomato str. dc3000]]
 [[Category: Sulfate adenylyltransferase]]
-[[Category: Berger, J.M.]]
+[[Category: Berger, J M.]]
-[[Category: Bertozzi, C.R.]]
+[[Category: Bertozzi, C R.]]
-[[Category: Hubbard, S.C.]]
+[[Category: Hubbard, S C.]]
-[[Category: Lee, D.H.]]
+[[Category: Lee, D H.]]
-[[Category: Mougous, J.D.]]
+[[Category: Mougous, J D.]]
-[[Category: Schelle, M.W.]]
+[[Category: Schelle, M W.]]
-[[Category: Vocadlo, D.J.]]
+[[Category: Vocadlo, D J.]]
 [[Category: AGS]]
 [[Category: GDP]]
@@ Line 33: / Line 33: @@
 [[Category: switch domain]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 07:40:21 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:19:13 2008''