Gaojie Song and Chongyun Cheng contributed equally to this work
Crystal structure of the N-terminal methyltransferase-like domain of anamorsin
Article first published online: 22 NOV 2013
Copyright © 2013 Wiley Periodicals, Inc.
Proteins: Structure, Function, and Bioinformatics
How to Cite
Song, G., Cheng, C., Li, Y., Shaw, N., Xiao, Z.-C. and Liu, Z.-J. (2013), Crystal structure of the N-terminal methyltransferase-like domain of anamorsin. Proteins. doi: 10.1002/prot.24443
- Article first published online: 22 NOV 2013
- Accepted manuscript online: 9 OCT 2013 01:05PM EST
- Manuscript Accepted: 26 SEP 2013
- Manuscript Revised: 19 SEP 2013
- Manuscript Received: 19 AUG 2013
- Ministry of Science and Technology of China . Grant Number: 2014CB910400
- crystal structure;
- methyltransferase-like fold
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 β-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.Proteins 2013. © 2013 Wiley Periodicals, Inc.