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==Crystal structure of T. brucei arginase-like protein quadruple mutant S149D/R151H/S153D/S226D== | ==Crystal structure of T. brucei arginase-like protein quadruple mutant S149D/R151H/S153D/S226D== | ||
<StructureSection load='4rhm' size='340' side='right' caption='[[4rhm]], [[Resolution|resolution]] 1.95Å' scene=''> | <StructureSection load='4rhm' size='340' side='right' caption='[[4rhm]], [[Resolution|resolution]] 1.95Å' scene=''> | ||
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4rhi|4rhi]], [[4rhj|4rhj]], [[4rhk|4rhk]], [[4rhl|4rhl]], [[4rhq|4rhq]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4rhi|4rhi]], [[4rhj|4rhj]], [[4rhk|4rhk]], [[4rhl|4rhl]], [[4rhq|4rhq]]</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4rhm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rhm OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4rhm RCSB], [http://www.ebi.ac.uk/pdbsum/4rhm PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4rhm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rhm OCA], [http://pdbe.org/4rhm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4rhm RCSB], [http://www.ebi.ac.uk/pdbsum/4rhm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4rhm ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 4rhm" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
Revision as of 16:28, 11 August 2016
Crystal structure of T. brucei arginase-like protein quadruple mutant S149D/R151H/S153D/S226DCrystal structure of T. brucei arginase-like protein quadruple mutant S149D/R151H/S153D/S226D
Structural highlights
Publication Abstract from PubMedThe X-ray crystal structure of an arginase-like protein from the parasitic protozoan Trypanosoma brucei, designated TbARG, is reported at 1.80 and 2.38 A resolution in its reduced and oxidized forms, respectively. The oxidized form of TbARG is a disulfide-linked hexamer that retains the overall architecture of a dimer of trimers in the reduced form. Intriguingly, TbARG does not contain metal ions in its putative active site, and amino acid sequence comparisons indicate that all but one of the residues required for coordination to the catalytically obligatory binuclear manganese cluster in other arginases are substituted here with residues incapable of metal ion coordination. Therefore, the structure of TbARG is the first of a member of the arginase/deacetylase superfamily that is not a metalloprotein. Although we show that metal binding activity is easily reconstituted in TbARG by site-directed mutagenesis and confirmed in X-ray crystal structures, it is curious that this protein and its parasitic orthologues evolved away from metal binding function. Knockout of the TbARG gene from the genome demonstrated that its function is not essential to cultured bloodstream-form T. brucei, and metabolomics analysis confirmed that the enzyme has no role in the conversion of l-arginine to l-ornithine in these cells. While the molecular function of TbARG remains enigmatic, the fact that the T. brucei genome encodes only this protein and not a functional arginase indicates that the parasite must import l-ornithine from its host to provide a source of substrate for ornithine decarboxylase in the polyamine biosynthetic pathway, an active target for the development of antiparasitic drugs. Crystal Structure of an Arginase-like Protein from Trypanosoma brucei That Evolved without a Binuclear Manganese Cluster.,Hai Y, Kerkhoven EJ, Barrett MP, Christianson DW Biochemistry. 2014 Dec 23. PMID:25536859[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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