3mbb

Crystal structure of StSPL - apo form, after treatment with semicarbazide

spinqualitylabelsall models 3mbb, resolution 2.05Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3mbb is a 2 chain structure with sequence from Symbiobacterium thermophilum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.051Å Ligands: EDO, NA, PO4, TY2 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q67PY4_SYMTH Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Sphingosine-1-phosphate lyase (SPL), a key enzyme of sphingolipid metabolism, catalyzes the irreversible degradation of sphingoid base phosphates. Its main substrate sphingosine-1-phosphate (S1P) acts both extracellularly, by binding G protein-coupled receptors of the lysophospholipid receptor family, and inside the cell, as a second messenger. There, S1P takes part in regulating various cellular processes and its levels are tightly regulated. SPL is a pivotal enzyme regulating S1P intracellular concentrations and a promising drug target for the design of immunosuppressants. We structurally and functionally characterized yeast SPL (Dpl1p) and its first prokaryotic homolog, from Symbiobacterium thermophilum. The Dpl1p structure served as a basis for a very reliable model of Homo sapiens SPL. The above results, together with in vitro and in vivo studies of SPL mutants, reveal which residues are involved in activity and substrate binding and pave the way to studies aimed at controlling the activity of this pivotal enzyme. Structure and function of sphingosine-1-phosphate lyase, a key enzyme of sphingolipid metabolism.,Bourquin F, Riezman H, Capitani G, Grutter MG Structure. 2010 Aug 11;18(8):1054-65. PMID:20696404 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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