5zeh: Difference between revisions
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New page: '''Unreleased structure''' The entry 5zeh is ON HOLD Authors: Malik, A., Dalal, V., Ankri, S., Tomar, S. Description: Crystal structure of Entamoeba histolytica Arginase in complex wit... |
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==Crystal structure of Entamoeba histolytica Arginase in complex with L- Ornithine at 2.35 A== | |||
<StructureSection load='5zeh' size='340' side='right'caption='[[5zeh]], [[Resolution|resolution]] 2.36Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5zeh]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Entamoeba_histolytica Entamoeba histolytica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZEH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ZEH 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]] 2.36Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=ORN:L-ORNITHINE'>ORN</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=5zeh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zeh OCA], [https://pdbe.org/5zeh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5zeh RCSB], [https://www.ebi.ac.uk/pdbsum/5zeh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5zeh ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/ARGI_ENTH1 ARGI_ENTH1] Catalyzes the hydrolysis of L-arginine into urea and L-ornithine, which is a precursor for polyamine biosynthesis (PubMed:15053781, PubMed:29691540, PubMed:31199070). By depleting host L-arginine, a substrate for nitric oxide synthase (NOS), prevents the production of nitric oxide (NO) by host activated macrophages, and thus allows the parasite to evade host immune response (PubMed:15053781).<ref>PMID:15053781</ref> <ref>PMID:29691540</ref> <ref>PMID:31199070</ref> | |||
==See Also== | |||
*[[Arginase 3D structures|Arginase 3D structures]] | |||
== References == | |||
[[Category: | <references/> | ||
[[Category: | __TOC__ | ||
[[Category: | </StructureSection> | ||
[[Category: | [[Category: Entamoeba histolytica]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Ankri S]] | |||
[[Category: Dalal V]] | |||
[[Category: Malik A]] | |||
[[Category: Tomar S]] | |||
Latest revision as of 13:27, 27 March 2024
Crystal structure of Entamoeba histolytica Arginase in complex with L- Ornithine at 2.35 ACrystal structure of Entamoeba histolytica Arginase in complex with L- Ornithine at 2.35 A
Structural highlights
FunctionARGI_ENTH1 Catalyzes the hydrolysis of L-arginine into urea and L-ornithine, which is a precursor for polyamine biosynthesis (PubMed:15053781, PubMed:29691540, PubMed:31199070). By depleting host L-arginine, a substrate for nitric oxide synthase (NOS), prevents the production of nitric oxide (NO) by host activated macrophages, and thus allows the parasite to evade host immune response (PubMed:15053781).[1] [2] [3] See AlsoReferences
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