1i2d: Difference between revisions

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-[[Image:1i2d.jpg|left|200px]]
- {{Structure
+==CRYSTAL STRUCTURE OF ATP SULFURYLASE FROM PENICILLIUM CHRYSOGENUM==
-|PDB= 1i2d |SIZE=350|CAPTION= <scene name='initialview01'>1i2d</scene>, resolution 2.81&Aring;
+<StructureSection load='1i2d' size='340' side='right'caption='[[1i2d]], [[Resolution|resolution]] 2.81&Aring;' scene=''>
-|SITE=
+== Structural highlights ==
-|LIGAND= <scene name='pdbligand=ADX:ADENOSINE-5&#39;-PHOSPHOSULFATE'>ADX</scene>
+<table><tr><td colspan='2'>[[1i2d]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Penicillium_chrysogenum Penicillium chrysogenum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I2D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1I2D 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]] 2.81&#8491;</td></tr>
-|GENE= APS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5076 Penicillium chrysogenum])
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADX:ADENOSINE-5-PHOSPHOSULFATE'>ADX</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=1i2d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i2d OCA], [https://pdbe.org/1i2d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1i2d RCSB], [https://www.ebi.ac.uk/pdbsum/1i2d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1i2d ProSAT]</span></td></tr>
+</table>
-'''CRYSTAL STRUCTURE OF ATP SULFURYLASE FROM PENICILLIUM CHRYSOGENUM'''
+== Function ==
+[https://www.uniprot.org/uniprot/MET3_PENCH MET3_PENCH] Catalyzes the first intracellular reaction of sulfate assimilation, forming adenosine-5'-phosphosulfate (APS) from inorganic sulfate and ATP. Plays an important role in sulfate activation as a component of the biosynthesis pathway of sulfur-containing amino acids.
+== Evolutionary Conservation ==
-==Overview==
+[[Image:Consurf_key_small.gif|200px|right]]
-ATP sulfurylase from Penicillium chrysogenum is an allosterically regulated enzyme composed of six identical 63.7 kDa subunits (573 residues). The C-terminal allosteric domain of each subunit is homologous to APS kinase. In the presence of APS, the enzyme crystallized in the orthorhombic space group (I222) with unit cell parameters of a = 135.7 A, b = 162.1 A, and c = 273.0 A. The X-ray structure at 2.8 A resolution established that the hexameric enzyme is a dimer of triads in the shape of an oblate ellipsoid 140 A diameter x 70 A. Each subunit is divided into a discreet N-terminal domain, a central catalytic domain, and a C-terminal allosteric domain. Two molecules of APS bound per subunit clearly identify the catalytic and allosteric domains. The sequence 197QXRN200 is largely responsible for anchoring the phosphosulfate group of APS at the active site of the catalytic domain. The specificity of the catalytic site for adenine nucleotides is established by specific hydrogen bonds to the protein main chain. APS was bound to the allosteric site through sequence-specific interactions with amino acid side chains that are conserved in true APS kinase. Within a given triad, the allosteric domain of one subunit interacts with the catalytic domain of another. There are also allosteric-allosteric, allosteric-N-terminal, and catalytic-catalytic domain interactions across the triad interface. The overall interactions-each subunit with four others-provide stability to the hexamer as well as a way to propagate a concerted allosteric transition. The structure presented here is believed to be the R state. A solvent channel, 15-70 A wide exists along the 3-fold axis, but substrates have access to the catalytic site only from the external medium. On the other hand, a surface "trench" links each catalytic site in one triad with an allosteric site in the other triad. This trench may be a vestigial feature of a bifunctional ("PAPS synthetase") ancestor of fungal ATP sulfurylase.
+Check<jmol>
+  <jmolCheckbox>
-==About this Structure==
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/i2/1i2d_consurf.spt"</scriptWhenChecked>
-I2D is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Penicillium_chrysogenum Penicillium chrysogenum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I2D OCA].
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
-==Reference==
+  </jmolCheckbox>
-Crystal structure of ATP sulfurylase from Penicillium chrysogenum: insights into the allosteric regulation of sulfate assimilation., MacRae IJ, Segel IH, Fisher AJ, Biochemistry. 2001 Jun 12;40(23):6795-804. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11389593 11389593]
+</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=1i2d ConSurf].
+<div style="clear:both"></div>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
 [[Category: Penicillium chrysogenum]]
-[[Category: Single protein]]
+[[Category: Fisher AJ]]
-[[Category: Sulfate adenylyltransferase]]
+[[Category: MacRae IJ]]
-[[Category: Fisher, A J.]]
+[[Category: Segel IH]]
-[[Category: MacRae, I J.]]
-[[Category: Segel, I H.]]
-[[Category: ADX]]
-[[Category: allosteric]]
-[[Category: hexamer]]
-[[Category: nucleotide binding]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 12:09:38 2008''