SAM (dependent) I AM: the S-adenosylmethionine-dependent methyltransferase fold
Data(s) |
01/01/2002
|
---|---|
Resumo |
The S-adenosylmethionine-dependent methyltransferase enzymes share little sequence identity, but incorporate a highly conserved structural fold. Surprisingly, residues that bind the common cofactor are poorly conserved, although the binding site is localised to the same region of the fold. The substrate-binding region of the fold varies enormously. Over the past two years, there has been a significant increase in the number of structures that are known to incorporate this fold, including several uncharacterised proteins and two proteins that lack methyltransferase activity. |
Identificador | |
Idioma(s) |
eng |
Publicador |
Elsevier Science - current Biology Ltd |
Palavras-Chave | #Biochemistry & Molecular Biology #Cell Biology #Ribosomal-rna Methyltransferase #Glycine N-methyltransferase #Hhai Dna Methyltransferase #Adenosyl-l-methionine #Crystal-structure #Messenger-rna #Arginine Methyltransferase #Antibiotic-resistance #Angstrom Structure #Protein Repair #C1 #270108 Enzymes #670403 Treatments (e.g. chemicals, antibiotics) |
Tipo |
Journal Article |