4M7R

Crystal structure of the N-terminal methyltransferase-like domain of anamorsin

Summary for 4M7R

• Entry DOI: 10.2210/pdb4m7r/pdb
• Descriptor: Anamorsin, MERCURY (II) ION (3 entities in total)
• Functional Keywords: rossmann fold, apoptosis
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm: Q6FI81
• Total number of polymer chains: 2
• Total formula weight: 42766.72

Authors

Song, G.,Liu, Z.-J. (deposition date: 2013-08-12, release date: 2013-10-30, Last modification date: 2024-05-29)

Primary citation

Song, G.,Cheng, C.,Li, Y.,Shaw, N.,Xiao, Z.C.,Liu, Z.J.
Crystal structure of the N-terminal methyltransferase-like domain of anamorsin.
Proteins, 82:1066-1071, 2014

PubMed 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 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.

PubMed: 24123282
DOI: 10.1002/prot.24443

Experimental method

X-RAY DIFFRACTION (1.801 Å)