3MBB

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

3MBB の概要

• エントリーDOI: 10.2210/pdb3mbb/pdb
• 関連するPDBエントリー: 3MAD 3MAF 3MAU 3MC6
• 分子名称: Putative sphingosine-1-phosphate lyase, PHOSPHATE ION, 1,2-ETHANEDIOL, ... (5 entities in total)
• 機能のキーワード: carboxy-lyase activity, pyridoxal phosphate, lyase
• 由来する生物種: Symbiobacterium thermophilum
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 111757.17

構造登録者

Bourquin, F.,Grutter, M.G.,Capitani, G. (登録日: 2010-03-25, 公開日: 2010-08-18, 最終更新日: 2024-11-06)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.051 Å)