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Recently, in the 1980's, the primary structure of sphingomyelinase was determined by cloning the first N-SMases from ''Bacillus cereus'' and ''Staphylococcus aureus'' and by the subsequent sequencing of their cDNAs <ref name="gp4">PMID: 2127932 </ref>.
Recently, in the 1980's, the primary structure of sphingomyelinase was determined by cloning the first N-SMases from ''Bacillus cereus'' and ''Staphylococcus aureus'' and by the subsequent sequencing of their cDNAs <ref name="gp4">PMID: 2127932 </ref>.
The crystal structure of sphingomyelinase has been solved using ''Listeria ivanovii'' and ''Bacillus cereus(Bc-SMase)'' to gain further insight into its catalytic activities <ref name="gp5">PMID: 16595670 </ref>.
The crystal structure of sphingomyelinase has been solved using ''Listeria ivanovii'' and ''Bacillus cereus(Bc-SMase)'' to gain further insight into its catalytic activities <ref name="gp5">PMID: 16595670 </ref>.
 +
=Mechanism=
=Mechanism=
 +
The mechanism of shingomyelinase catalytic activity is not fully understood in atomic detail because the cystal structures of SMase in complex with the essential divalent metal ions, Co2+, Mn2+, Mg2+, Ca2+, and Sr2+, has not been clarified <ref name="gp5">PMID: 16595670 </ref>.
=Importance of SMase=
=Importance of SMase=
=References=
=References=
<references/>
<references/>

Revision as of 16:47, 23 March 2011

This Sandbox is Reserved from January 10, 2010, through April 10, 2011 for use in BCMB 307-Proteins course taught by Andrea Gorrell at the University of Northern British Columbia, Prince George, BC, Canada.
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PDB ID 2dds

Drag the structure with the mouse to rotate
2dds, resolution 1.80Å ()
Ligands:
Activity: Sphingomyelin phosphodiesterase, with EC number 3.1.4.12
Related: 2ddr, 2ddt
Resources: FirstGlance, OCA, PDBsum, RCSB, TOPSAN
Coordinates: save as pdb, mmCIF, xml


Contents

Introduction

Sphingomyelin phosphodiesterase (Sphingomyelinase): (SMase) is an enzyme which catalyzes the hydrolysis of sphingomyelin to ceramide and phosphocholine [1]. This enzyme has become the object of renewed interest since the discovery of the sphingomyelin signal transduction pathway which is involved in apoptosis. This pathway is initiated by a neutral sphingomyelinase hydrolysis of sphingomyelin in the plasma membrane to generate ceramide. Ceramide acts as a secondary messenger which causes the stimulation of the cascade effect of kinases and transcription factors which activate programmed cell death[2]. There are 6 known types of sphingomyelinases[3]. :

Acid sphingomyelinase (aSMase) -

Secretory sphingomyelinase (sSMase) -

Neutral Mg2+-dependent sphingomyelinases (nSMase) -

Neutral Mg2+-independent sphingomyelinases -

Alkaline sphingomyelinase -

Bacterial sphingomyelinase -

Structure and Function

Recently, in the 1980's, the primary structure of sphingomyelinase was determined by cloning the first N-SMases from Bacillus cereus and Staphylococcus aureus and by the subsequent sequencing of their cDNAs [4]. The crystal structure of sphingomyelinase has been solved using Listeria ivanovii and Bacillus cereus(Bc-SMase) to gain further insight into its catalytic activities [5].

Mechanism

The mechanism of shingomyelinase catalytic activity is not fully understood in atomic detail because the cystal structures of SMase in complex with the essential divalent metal ions, Co2+, Mn2+, Mg2+, Ca2+, and Sr2+, has not been clarified [5].

Importance of SMase

References

  1. ↑ Ago H, Oda M, Takahashi M, Tsuge H, Ochi S, Katunuma N, Miyano M, Sakurai J. Structural basis of the sphingomyelin phosphodiesterase activity in neutral sphingomyelinase from Bacillus cereus. J Biol Chem. 2006 Jun 9;281(23):16157-67. Epub 2006 Apr 4. PMID:16595670 doi:10.1074/jbc.M601089200
  2. ↑ Kolesnick RN, Haimovitz-Friedman A, Fuks Z. The sphingomyelin signal transduction pathway mediates apoptosis for tumor necrosis factor, Fas, and ionizing radiation. Biochem Cell Biol. 1994 Nov-Dec;72(11-12):471-4. PMID:7544586
  3. ↑ Goni FM, Alonso A. Sphingomyelinases: enzymology and membrane activity. FEBS Lett. 2002 Oct 30;531(1):38-46. PMID:12401200
  4. ↑ Tomita M, Nakai K, Yamada A, Taguchi R, Ikezawa H. Secondary structure of sphingomyelinase from Bacillus cereus. J Biochem. 1990 Nov;108(5):811-5. PMID:2127932
  5. ↑ 5.0 5.1 Ago H, Oda M, Takahashi M, Tsuge H, Ochi S, Katunuma N, Miyano M, Sakurai J. Structural basis of the sphingomyelin phosphodiesterase activity in neutral sphingomyelinase from Bacillus cereus. J Biol Chem. 2006 Jun 9;281(23):16157-67. Epub 2006 Apr 4. PMID:16595670 doi:10.1074/jbc.M601089200
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