1ta1: Difference between revisions

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OCA

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-[[Image:1ta1.gif|left|200px]]<br /><applet load="1ta1" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1ta1, resolution 2.50&Aring;" />
-'''H141C mutant of rat liver arginase I'''<br />
-==Overview==
+==H141C mutant of rat liver arginase I==
-Rat liver arginase (arginase I) is potently inactivated by diethyl, pyrocarbonate, with a second-order rate constant of 113M(-1)s(-1) for the, inactivation process at pH 7.0, 25 degrees C. Partial protection from, inactivation is provided by the product of the reaction, l-ornithine, while nearly complete protection is afforded by the inhibitor pair, l-ornithine and borate. The role of H141 has been probed by mutagenesis, chemical modulation, and X-ray diffraction. The hyper-reactivity of H141, towards diethyl pyrocarbonate can be explained by its proximity to E277. A, proton shuttling role for H141 is supported by its conformational mobility, observed among the known arginase structures. H141 is proposed to serve as, an acid/base catalyst, deprotonating the metal-bridging water molecule to, generate the metal-bridging hydroxide nucleophile, and by protonating the, amino group of the product to facilitate its departure.
+<StructureSection load='1ta1' size='340' side='right'caption='[[1ta1]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1ta1]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TA1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TA1 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]] 2.5&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</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=1ta1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ta1 OCA], [https://pdbe.org/1ta1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ta1 RCSB], [https://www.ebi.ac.uk/pdbsum/1ta1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ta1 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/ARGI1_RAT ARGI1_RAT]
+== 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/ta/1ta1_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=1ta1 ConSurf].
+<div style="clear:both"></div>
-==About this Structure==
+==See Also==
-TA1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with MN and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Arginase Arginase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.3.1 3.5.3.1] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1TA1 OCA].
+*[[Arginase 3D structures|Arginase 3D structures]]
+__TOC__
-==Reference==
+</StructureSection>
-Probing the role of the hyper-reactive histidine residue of arginase., Colleluori DM, Reczkowski RS, Emig FA, Cama E, Cox JD, Scolnick LR, Compher K, Jude K, Han S, Viola RE, Christianson DW, Ash DE, Arch Biochem Biophys. 2005 Dec 1;444(1):15-26. Epub 2005 Oct 13. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16266687 16266687]
+[[Category: Large Structures]]
-[[Category: Arginase]]
 [[Category: Rattus norvegicus]]
-[[Category: Single protein]]
+[[Category: Ash DE]]
-[[Category: Ash, D.E.]]
+[[Category: Cama E]]
-[[Category: Cama, E.]]
+[[Category: Christianson DW]]
-[[Category: Christianson, D.W.]]
+[[Category: Cox JD]]
-[[Category: Cox, J.D.]]
-[[Category: GOL]]
-[[Category: MN]]
-[[Category: arginase]]
-[[Category: binuclear manganese cluster]]
-[[Category: h141c mutation]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 03:06:41 2007''