1ta1
From Proteopedia
(Difference between revisions)
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<StructureSection load='1ta1' size='340' side='right'caption='[[1ta1]], [[Resolution|resolution]] 2.50Å' scene=''> | <StructureSection load='1ta1' size='340' side='right'caption='[[1ta1]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1ta1]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <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=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5Å</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=' | + | |
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<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> | <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> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/ARGI1_RAT ARGI1_RAT] | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</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]. | </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> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | 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. | ||
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| - | 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:16266687<ref>PMID:16266687</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1ta1" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Arginase 3D structures|Arginase 3D structures]] | *[[Arginase 3D structures|Arginase 3D structures]] | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: Arginase]] | ||
| - | [[Category: Buffalo rat]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: | + | [[Category: Rattus norvegicus]] |
| - | [[Category: | + | [[Category: Ash DE]] |
| - | [[Category: | + | [[Category: Cama E]] |
| - | [[Category: | + | [[Category: Christianson DW]] |
| - | [[Category: | + | [[Category: Cox JD]] |
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Current revision
H141C mutant of rat liver arginase I
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