Crystal structure of the N-terminal methyltransferase-like domain of anamorsin.
Proteins
; 82(6): 1066-71, 2014 Jun.
Article
em En
| MEDLINE
| ID: mdl-24123282
ABSTRACT
Anamorsin is a recently identified molecule that inhibits apoptosis during hematopoiesis. It contains an N-terminal methyltransferase-like domain and a C-terminal Fe-S cluster motif. Not much is known about the function of the protein. To better understand the function of anamorsin, we have solved the crystal structure of the N-terminal domain at 1.8 Å resolution. Although the overall structure resembles a typical S-adenosylmethionine (SAM) dependent methyltransferase fold, it lacks one α-helix and one ß-strand. As a result, the N-terminal domain as well as the full-length anamorsin did not show S-adenosyl-L-methionine (AdoMet) dependent methyltransferase activity. Structural comparisons with known AdoMet dependent methyltransferases reveals subtle differences in the SAM binding pocket that preclude the N-terminal domain from binding to AdoMet. The N-terminal methyltransferase-like domain of anamorsin probably functions as a structural scaffold to inhibit methyl transfers by out-competing other AdoMet dependant methyltransferases or acts as bait for protein-protein interactions.
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Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Peptídeos e Proteínas de Sinalização Intracelular
/
Metiltransferases
Limite:
Humans
Idioma:
En
Ano de publicação:
2014
Tipo de documento:
Article