5zeh: Difference between revisions

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'''Unreleased structure'''


The entry 5zeh is ON HOLD
==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]] 2.36&Aring;' 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]] 2.36&#8491;</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>


Authors: Malik, A., Dalal, V., Ankri, S., Tomar, S.
==See Also==
 
*[[Arginase 3D structures|Arginase 3D structures]]
Description: Crystal structure of Entamoeba histolytica Arginase in complex with L-Ornithine at 2.35 A
== References ==
[[Category: Unreleased Structures]]
<references/>
[[Category: Dalal, V]]
__TOC__
[[Category: Tomar, S]]
</StructureSection>
[[Category: Ankri, S]]
[[Category: Entamoeba histolytica]]
[[Category: Malik, A]]
[[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

5zeh is a 2 chain structure with sequence from Entamoeba histolytica. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.36Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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).[1] [2] [3]

See Also

References

  1. Elnekave K, Siman-Tov R, Ankri S. Consumption of L-arginine mediated by Entamoeba histolytica L-arginase (EhArg) inhibits amoebicidal activity and nitric oxide production by activated macrophages. Parasite Immunol. 2003 Nov-Dec;25(11-12):597-608. PMID:15053781 doi:10.1111/j.0141-9838.2004.00669.x
  2. Malik A, Singh H, Pareek A, Tomar S. Biochemical and biophysical insights into the metal binding spectrum and bioactivity of arginase of Entamoeba histolytica. Metallomics. 2018 Apr 25;10(4):623-638. PMID:29691540 doi:10.1039/c8mt00002f
  3. Malik A, Dalal V, Ankri S, Tomar S. Structural insights into Entamoeba histolytica arginase and structure-based identification of novel non-amino acid based inhibitors as potential antiamoebic molecules. FEBS J. 2019 Jun 14. doi: 10.1111/febs.14960. PMID:31199070 doi:http://dx.doi.org/10.1111/febs.14960

5zeh, resolution 2.36Å

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