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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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spinqualitylabelsall models PDB ID 2dds Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image
2dds, resolution 1.80Å ()
Ligands:
Activity:	Sphingomyelin phosphodiesterase, with EC number 3.1.4.12
Related:	2ddr, 2ddt
Structural annotation: Resources: InterPro : Ipr005135 Pfam : PF03372 UniProt : P11889
Functional annotation: Biological process: cytolysis hemolysis by symbiont of host red blood cells Molecular function: sphingomyelin phosphodiesterase activity hydrolase activity
Evolutionary conservation: Toggle Conservation Colors: Rows = identical sequences: Further Information: Caveats, Explanation, Complete Results at ConSurfDB
Resources:	FirstGlance, OCA, PDBsum, RCSB, TOPSAN
Coordinates:	save as pdb, mmCIF, xml

Contents 1 Introduction 1.1 Acid sphingomyelinase (aSMase) 1.2 Neutral, Mg2+-dependent sphingomyelinases (nSMase) 1.3 Mg2+-independent neutral sphingomyelinases. 1.4 Alkaline sphingomyelinase 1.5 Bacterial sphingomyelinase 2 Structure and Function 3 Mechanism 4 Importance of SMase 5 References

Introduction

Sphingomyelin phosphodiesterase (SMase) is an enzyme which catalyzes the hydrolysis of sphingomyelin to ceramide and phosphocholine ^[1]. There are 6 known types of sphingomyelinases:

Acid sphingomyelinase (aSMase)

==Secretory sphingomyelinase (sSMase)

Neutral, Mg2+-dependent sphingomyelinases (nSMase)

Mg2+-independent neutral sphingomyelinases.

Alkaline sphingomyelinase

Bacterial sphingomyelinase

Structure and Function

Mechanism

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