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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