1i5o: Difference between revisions

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-[[Image:1i5o.gif|left|200px]]
- {{Structure
+==CRYSTAL STRUCTURE OF MUTANT R105A OF E. COLI ASPARTATE TRANSCARBAMOYLASE==
-|PDB= 1i5o |SIZE=350|CAPTION= <scene name='initialview01'>1i5o</scene>, resolution 2.8&Aring;
+<StructureSection load='1i5o' size='340' side='right'caption='[[1i5o]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
-|SITE=
+== Structural highlights ==
-|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> and <scene name='pdbligand=PAL:N-(PHOSPHONACETYL)-L-ASPARTIC ACID'>PAL</scene>
+<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>
-|ACTIVITY= [http://en.wikipedia.org/wiki/Aspartate_carbamoyltransferase Aspartate carbamoyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.3.2 2.1.3.2]
+</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>
-|GENE= PYRB, PYRI ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
+<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.
-'''CRYSTAL STRUCTURE OF MUTANT R105A OF E. COLI ASPARTATE TRANSCARBAMOYLASE'''
+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>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 1i5o" style="background-color:#fffaf0;"></div>
-==Overview==
+==See Also==
-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.
+*[[Aspartate carbamoyltransferase 3D structures|Aspartate carbamoyltransferase 3D structures]]
+== References ==
-==About this Structure==
+<references/>
-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].
+__TOC__
+</StructureSection>
-==Reference==
-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]
-[[Category: Aspartate carbamoyltransferase]]
 [[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: PAL]]
-[[Category: ZN]]
-[[Category: mutant aspartate transcarbamoylase]]
-[[Category: pala at the regulatory site]]
-[[Category: t-state]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:45:52 2008''