SAM (dependent) I AM: the S-adenosylmethionine-dependent methyltransferase fold


Autoria(s): Martin, Jennifer L.; McMillan, Fiona M.
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

http://espace.library.uq.edu.au/view/UQ:64176

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