6tor

human O-phosphoethanolamine phospho-lyase

spinqualitylabelsall models 6tor, resolution 2.05Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6tor is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.05Å Ligands: GOL, PMP Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function AT2L1_HUMAN Catalyzes the pyridoxal-phosphate-dependent breakdown of phosphoethanolamine, converting it to ammonia, inorganic phosphate and acetaldehyde. Publication Abstract from PubMed Human O-phosphoethanolamine phospho-lyase (hEtnppl; EC 4.2.3.2) is a pyridoxal 5'-phosphate-dependent enzyme that catalyzes the degradation of O-phosphoethanolamine (PEA) into acetaldehyde, phosphate and ammonia. Physiologically, the enzyme is involved in phospholipid metabolism, as PEA is the precursor of phosphatidylethanolamine in the CDP-ethanolamine (Kennedy) pathway. Here, the crystal structure of hEtnppl in complex with pyridoxamine 5'-phosphate was determined at 2.05 A resolution by molecular replacement using the structure of A1RDF1 from Arthrobacter aurescens TC1 (PDB entry 5g4i) as the search model. Structural analysis reveals that the two proteins share the same general fold and a similar arrangement of active-site residues. These results provide novel and useful information for the complete characterization of the human enzyme. Structural characterization of human O-phosphoethanolamine phospho-lyase.,Vettraino C, Peracchi A, Donini S, Parisini E Acta Crystallogr F Struct Biol Commun. 2020 Apr 1;76(Pt 4):160-167. doi:, 10.1107/S2053230X20002988. Epub 2020 Apr 1. PMID:32254049 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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