1i5o: Difference between revisions

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-[[Image:1i5o.gif|left|200px]]
-<!--
-The line below this paragraph, containing "STRUCTURE_1i5o", creates the "Structure Box" on the page.
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-or leave the SCENE parameter empty for the default display.
--->
-{{STRUCTURE_1i5o|  PDB=1i5o  |  SCENE=  }}
-'''CRYSTAL STRUCTURE OF MUTANT R105A OF E. COLI ASPARTATE TRANSCARBAMOYLASE'''
+==CRYSTAL STRUCTURE OF MUTANT R105A OF E. COLI ASPARTATE TRANSCARBAMOYLASE==
+<StructureSection load='1i5o' size='340' side='right'caption='[[1i5o]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1i5o]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I5O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1I5O FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PAL:N-(PHOSPHONACETYL)-L-ASPARTIC+ACID'>PAL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=1i5o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i5o OCA], [https://pdbe.org/1i5o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1i5o RCSB], [https://www.ebi.ac.uk/pdbsum/1i5o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1i5o ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/PYRB_ECOLI PYRB_ECOLI]
+== Evolutionary Conservation ==
+[[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/i5/1i5o_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=1i5o ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Regulation of protein function, often achieved by allosteric mechanisms, is central to normal physiology and cellular processes. Although numerous models have been proposed to account for the cooperative binding of ligands to allosteric proteins and enzymes, direct structural support has been lacking. Here, we used a combination of X-ray crystallography and small angle X-ray scattering in solution to provide direct structural evidence that the binding of ligand to just one of the six active sites of Escherichia coli aspartate transcarbamoylase induces a concerted structural transition from the T to the R state.
-==Overview==
+Direct structural evidence for a concerted allosteric transition in Escherichia coli aspartate transcarbamoylase.,Macol CP, Tsuruta H, Stec B, Kantrowitz ER Nat Struct Biol. 2001 May;8(5):423-6. PMID:11323717<ref>PMID:11323717</ref>
-Regulation of protein function, often achieved by allosteric mechanisms, is central to normal physiology and cellular processes. Although numerous models have been proposed to account for the cooperative binding of ligands to allosteric proteins and enzymes, direct structural support has been lacking. Here, we used a combination of X-ray crystallography and small angle X-ray scattering in solution to provide direct structural evidence that the binding of ligand to just one of the six active sites of Escherichia coli aspartate transcarbamoylase induces a concerted structural transition from the T to the R state.
-==About this Structure==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-I5O is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I5O OCA].
+</div>
+<div class="pdbe-citations 1i5o" style="background-color:#fffaf0;"></div>
-==Reference==
+==See Also==
-Direct structural evidence for a concerted allosteric transition in Escherichia coli aspartate transcarbamoylase., Macol CP, Tsuruta H, Stec B, Kantrowitz ER, Nat Struct Biol. 2001 May;8(5):423-6. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11323717 11323717]
+*[[Aspartate carbamoyltransferase 3D structures|Aspartate carbamoyltransferase 3D structures]]
-[[Category: Aspartate carbamoyltransferase]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
 [[Category: Escherichia coli]]
-[[Category: Protein complex]]
+[[Category: Large Structures]]
-[[Category: Kantrowitz, E R.]]
+[[Category: Kantrowitz ER]]
-[[Category: Macol, C P.]]
+[[Category: Macol CP]]
-[[Category: Stec, B.]]
+[[Category: Stec B]]
-[[Category: Tsuruta, H.]]
+[[Category: Tsuruta H]]
-[[Category: Mutant aspartate transcarbamoylase]]
-[[Category: Pala at the regulatory site]]
-[[Category: T-state]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 19:36:22 2008''