5CVE: Crystal Structure Of Human Nrmt1 In Complex With Dimethylated Fly H2b Peptide And Sah

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 A. 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 A costructure of human NRMT1 bound to the fruit fly H2B peptide, underscore the importance of the NRMT1 recognition motif.
PDB ID: 5CVEDownload
MMDB ID: 134429
PDB Deposition Date: 2015/7/26
Updated in MMDB: 2015/12
Experimental Method:
x-ray diffraction
Resolution: 1.5  Å
Source Organism:
Homo sapiens
Similar Structures:
Biological Unit for 5CVE: dimeric; determined by author and by software (PISA)
Molecular Components in 5CVE
Label Count Molecule
Proteins (2 molecules)
N-terminal Xaa-pro-lys N-methyltransferase 1(Gene symbol: NTMT1)
Molecule annotation
N-terminal Peptide From Histone H2B(Gene symbol: His2B:CG17949)
Molecule annotation
Chemical (1 molecule)
* Click molecule labels to explore molecular sequence information.

Citing MMDB