4ylg | pdb_00004ylg

Structure of an ADP ribosylation factor from Entamoeba histolytica HM-1:IMSS bound to Mg-GDP

spinqualitylabelsall models 4ylg, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4ylg is a 2 chain structure with sequence from Entamoeba histolytica HM-1:IMSS. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.8Å Ligands: GDP, MG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function C4LXL1_ENTH1 GTP-binding protein involved in protein trafficking; modulates vesicle budding and uncoating within the Golgi apparatus.[RuleBase:RU369003] Publication Abstract from PubMed Entamoeba histolytica is the etiological agent of amebiasis, a diarrheal disease which causes amoebic liver abscesses and amoebic colitis. Approximately 50 million people are infected worldwide with E. histolytica. With only 10% of infected people developing symptomatic amebiasis, there are still an estimated 100 000 deaths each year. Because of the emergence of resistant strains of the parasite, it is necessary to find a treatment which would be a proper response to this challenge. ADP-ribosylation factor (ARF) is a member of the ARF family of GTP-binding proteins. These proteins are ubiquitous in eukaryotic cells; they generally associate with cell membranes and regulate vesicular traffic and intracellular signalling. The crystal structure of ARF1 from E. histolytica has been determined bound to magnesium and GDP at 1.8 A resolution. Comparison with other structures of eukaryotic ARF proteins shows a highly conserved structure and supports the interswitch toggle mechanism of communicating the conformational state to partner proteins. Structure of an ADP-ribosylation factor, ARF1, from Entamoeba histolytica bound to Mg(2+)-GDP.,Serbzhinskiy DA, Clifton MC, Sankaran B, Staker BL, Edwards TE, Myler PJ Acta Crystallogr F Struct Biol Commun. 2015 May;71(Pt 5):594-9. doi:, 10.1107/S2053230X15004677. Epub 2015 Apr 21. PMID:25945714 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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