5zbt

Structure of legume lectin-like domain from Entamoeba histolytica

spinqualitylabelsall models 5zbt, resolution 2.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5zbt is a 1 chain structure with sequence from Entamoeba histolytica HM-1:IMSS-A. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.4Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function N9T8S1_ENTH1 Publication Abstract from PubMed ERGIC-53-like proteins are type I membrane proteins that belong to the class of intracellular cargo receptors and are known to be indispensable for the intracellular transport of glycoproteins. They are implicated in transporting glycoproteins between the endoplasmic reticulum and the Golgi body. The crystal structure of the legume lectin-like domain of an ERGIC-53-like protein from Entamoeba histolytica has been determined at 2.4 A resolution. Although the overall structure of the domain resembles those of its mammalian and yeast orthologs (ERGIC-53 and Emp46, respectively), there are significant changes in the carbohydrate-binding site. A sequence-based search revealed the presence of several homologs of ERGIC-53 in different species of Entamoeba. This is the first report of the structural characterization of a member of this class of proteins from a protozoan and serves to further knowledge and understanding regarding the species-specific differences. Crystal structure of the legume lectin-like domain of an ERGIC-53-like protein from Entamoeba histolytica.,Khan F, Suguna K Acta Crystallogr F Struct Biol Commun. 2019 Mar 1;75(Pt 3):197-204. doi:, 10.1107/S2053230X19000499. Epub 2019 Feb 21. PMID:30839295 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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