 |
PDBsum entry 5cve
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Transferase/peptide
|
PDB id
|
|
|
|
5cve
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
Molecular basis for histone n-Terminal methylation by nrmt1.
|
|
|
Authors
|
|
R.Wu,
Y.Yue,
X.Zheng,
H.Li.
|
|
|
Ref.
|
|
Genes Dev, 2015,
29,
2337-2342.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
|
Abstract
|
|
|
NRMT1 is an N-terminal methyltransferase that methylates histone CENP-A as well
as nonhistone substrates. Here, we report the crystal structure of human NRMT1
bound to CENP-A peptide at 1.3 Å. NRMT1 adopts a core methyltransferase fold
that resembles DOT1L and PRMT but not SET domain family histone
methyltransferases. Key substrate recognition and catalytic residues were
identified by mutagenesis studies. Histone peptide profiling revealed that human
NRMT1 is highly selective to human CENP-A and fruit fly H2B, which share a
common "Xaa-Pro-Lys/Arg" motif. These results, along with a 1.5 Å
costructure of human NRMT1 bound to the fruit fly H2B peptide, underscore the
importance of the NRMT1 recognition motif.
|
|
|
|
|
|
|
