Sandbox Reserved 497: Difference between revisions

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==Structure==

The structure of DmdA has recently been solved through the use of X-Ray diffraction <ref> 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). </ref>. The structure is composed of 369 amino acid residues and contains three distinct domains and four ligands, two of which are sodium ions and two of which are glycerol. While DmdA belongs to the glycine cleavage T-protein (GcvT) family there is only approximately 25% sequence identify. These few conserved amino acids likely interact with tetrahydrofolate (THF), which is a cofactor required by DmdA as well as many other enzymes in the GcvT family.

The structure of DmdA has recently been solved through the use of X-Ray diffraction <ref> 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). </ref>. The structure is composed of 369 amino acid residues and contains three distinct domains and four <scene name='Sandbox_Reserved_497/Ligand/1'>ligands</scene>, two of which are sodium ions and two of which are glycerol. While DmdA belongs to the glycine cleavage T-protein (GcvT) family there is only approximately 25% sequence identify. These few conserved amino acids likely interact with tetrahydrofolate (THF), which is a cofactor required by DmdA as well as many other enzymes in the GcvT family.

==Mechanism of Action==

Sandbox Reserved 497: Difference between revisions

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@@ Line 12: / Line 12: @@
 ==Structure==
-The structure of DmdA has recently been solved through the use of X-Ray diffraction <ref> 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). </ref>. The structure is composed of 369 amino acid residues and contains three distinct domains and four ligands, two of which are sodium ions and two of which are glycerol. While DmdA belongs to the glycine cleavage T-protein (GcvT) family there is only approximately 25% sequence identify. These few conserved amino acids likely interact with tetrahydrofolate (THF), which is a cofactor required by DmdA as well as many other enzymes in the GcvT family.
+The structure of DmdA has recently been solved through the use of X-Ray diffraction <ref> 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). </ref>. The structure is composed of 369 amino acid residues and contains three distinct domains and four <scene name='Sandbox_Reserved_497/Ligand/1'>ligands</scene>, two of which are sodium ions and two of which are glycerol. While DmdA belongs to the glycine cleavage T-protein (GcvT) family there is only approximately 25% sequence identify. These few conserved amino acids likely interact with tetrahydrofolate (THF), which is a cofactor required by DmdA as well as many other enzymes in the GcvT family.
 ==Mechanism of Action==