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Sandbox Reserved 497

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Image from the RCSB PDB (www.pdb.org) of PDB ID 3TFH (Schuller, D.J., Reisch, C.R., Moran, M.A., Whitman, W.B., Lanzilotta, W.N. (2012) Structures of dimethylsulfoniopropinate-dependent demethylase from the marine organism pelagabacter ubique. Protein Sci. 21: 289-298).
 
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Schuller, D.J., Reisch, C.R., Moran, M.A., Whitman, W.B., Lanzilotta, W.N. (2012) Structures of dimethylsulfoniopropinate-dependent demethylase from the marine organism pelagabacter ubique. Protein Sci. 21: 289-298.
 

Revision as of 15:19, 1 May 2012

This Sandbox is Reserved from 13/03/2012, through 01/06/2012 for use in the course "Proteins and Molecular Mechanisms" taught by Robert B. Rose at the North Carolina State University, Raleigh, NC USA. This reservation includes Sandbox Reserved 451 through Sandbox Reserved 500.
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Contents

Dimethylsulfoniopropionate-Dependent Demethylase A (DmdA))

Dimethylsulfoniopropionate-Dependent Demethylase A (DmdA), 3TFH

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Introduction

Dimethylsulfoniopropionate-Dependendent Demethylase A (DmdA) is an enzyme produced by marine bacterioplankton in order to demethylate Dimethylsulfoniopropionate (DMSP).

Structure

The structure of DmdA was recently solved through X-Ray Diffraction [1]. The structure contains 369 amino acids folded into four domains and containing two ligands.

Mechanism of Action

The specific mechanism of DmdA is still being investigated. However, a mechanism was recently proposed [2]

Thumb

Possible Applications

References

  1. ↑ Image from the RCSB PDB (www.pdb.org) of PDB ID 3TFH (Schuller, D.J., Reisch, C.R., Moran, M.A., Whitman, W.B., Lanzilotta, W.N. (2012) Structures of dimethylsulfoniopropinate-dependent demethylase from the marine organism pelagabacter ubique. Protein Sci. 21: 289-298).
  2. ↑ Schuller, D.J., Reisch, C.R., Moran, M.A., Whitman, W.B., Lanzilotta, W.N. (2012) Structures of dimethylsulfoniopropinate-dependent demethylase from the marine organism pelagabacter ubique. Protein Sci. 21: 289-298.
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