3MAU

Crystal structure of StSPL in complex with phosphoethanolamine

Summary for 3MAU

• Entry DOI: 10.2210/pdb3mau/pdb
• Related: 3MAD 3MAF 3MBB 3MC6
• Descriptor: sphingosine-1-phosphate lyase, (5-HYDROXY-4,6-DIMETHYLPYRIDIN-3-YL)METHYL DIHYDROGEN PHOSPHATE, PHOSPHATE ION, ... (5 entities in total)
• Functional Keywords: carboxy-lyase activity, pyridoxyl phosphate, lyase
• Biological source: Symbiobacterium thermophilum
• Total number of polymer chains: 4
• Total formula weight: 223730.68

Authors

Bourquin, F.,Grutter, M.G.,Capitani, G. (deposition date: 2010-03-24, release date: 2010-08-18, Last modification date: 2024-02-21)

Primary citation

Bourquin, F.,Riezman, H.,Capitani, G.,Grutter, M.G.
Structure and Function of Sphingosine-1-Phosphate Lyase, a Key Enzyme of Sphingolipid Metabolism.
Structure, 18:1054-1065, 2010

PubMed Abstract: 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.

PubMed: 20696404
DOI: 10.1016/j.str.2010.05.011

Experimental method

X-RAY DIFFRACTION (2.9 Å)