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

(Difference between revisions)
Jump to: navigation, search
Current revision (08:13, 15 May 2024) (edit) (undo)
 
(13 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1zun.gif|left|200px]]
 
-
{{Structure
+
==Crystal Structure of a GTP-Regulated ATP Sulfurylase Heterodimer from Pseudomonas syringae==
-
|PDB= 1zun |SIZE=350|CAPTION= <scene name='initialview01'>1zun</scene>, resolution 2.70&Aring;
+
<StructureSection load='1zun' size='340' side='right'caption='[[1zun]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
-
|SITE=
+
== Structural highlights ==
-
|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>
+
<table><tr><td colspan='2'>[[1zun]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_syringae Pseudomonas syringae] and [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZUN FirstGlance]. <br>
-
|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]
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7&#8491;</td></tr>
-
|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])
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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></td></tr>
-
}}
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1zun FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zun OCA], [https://pdbe.org/1zun PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zun RCSB], [https://www.ebi.ac.uk/pdbsum/1zun PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zun ProSAT]</span></td></tr>
-
 
+
</table>
-
'''Crystal Structure of a GTP-Regulated ATP Sulfurylase Heterodimer from Pseudomonas syringae'''
+
== Function ==
-
 
+
[https://www.uniprot.org/uniprot/CYSD_PSESM CYSD_PSESM]
-
 
+
== Evolutionary Conservation ==
-
==Overview==
+
[[Image:Consurf_key_small.gif|200px|right]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/zu/1zun_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 +
<text>to colour the structure by Evolutionary Conservation</text>
 +
</jmolCheckbox>
 +
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1zun ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
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==
+
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<ref>PMID:16387658</ref>
-
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==
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
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]
+
</div>
-
[[Category: Protein complex]]
+
<div class="pdbe-citations 1zun" style="background-color:#fffaf0;"></div>
 +
== References ==
 +
<references/>
 +
__TOC__
 +
</StructureSection>
 +
[[Category: Large Structures]]
[[Category: Pseudomonas syringae]]
[[Category: Pseudomonas syringae]]
-
[[Category: Pseudomonas syringae pv. tomato str. dc3000]]
+
[[Category: Pseudomonas syringae pv. tomato str. DC3000]]
-
[[Category: Sulfate adenylyltransferase]]
+
[[Category: Berger JM]]
-
[[Category: Berger, J M.]]
+
[[Category: Bertozzi CR]]
-
[[Category: Bertozzi, C R.]]
+
[[Category: Hubbard SC]]
-
[[Category: Hubbard, S C.]]
+
[[Category: Lee DH]]
-
[[Category: Lee, D H.]]
+
[[Category: Mougous JD]]
-
[[Category: Mougous, J D.]]
+
[[Category: Schelle MW]]
-
[[Category: Schelle, M W.]]
+
[[Category: Vocadlo DJ]]
-
[[Category: Vocadlo, D J.]]
+
-
[[Category: AGS]]
+
-
[[Category: GDP]]
+
-
[[Category: MG]]
+
-
[[Category: NA]]
+
-
[[Category: beta barrel]]
+
-
[[Category: g protein]]
+
-
[[Category: gtpase]]
+
-
[[Category: heterodimer]]
+
-
[[Category: pyrophosphate]]
+
-
[[Category: switch domain]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:40:01 2008''
+

Current revision

Crystal Structure of a GTP-Regulated ATP Sulfurylase Heterodimer from Pseudomonas syringae

PDB ID 1zun

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1zun"
Personal tools