5CVE

Crystal Structure of human NRMT1 in complex with dimethylated fly H2B peptide and SAH

Summary for 5CVE

• Entry DOI: 10.2210/pdb5cve/pdb
• Related: 5CVD
• Descriptor: N-terminal Xaa-Pro-Lys N-methyltransferase 1, N-terminal peptide from Histone H2B, S-ADENOSYL-L-HOMOCYSTEINE, ... (4 entities in total)
• Functional Keywords: n-terminal methyltransferase, transferase-peptide complex, transferase/peptide
• Biological source: Homo sapiens (Human); More
• Cellular location: Nucleus : Q9BV86 P02283
• Total number of polymer chains: 4
• Total formula weight: 57721.77

Authors

Wu, R.,Li, H. (deposition date: 2015-07-26, release date: 2015-11-25, Last modification date: 2017-09-27)

Primary citation

Wu, R.,Yue, Y.,Zheng, X.,Li, H.
Molecular basis for histone N-terminal methylation by NRMT1
Genes Dev., 29:2337-2342, 2015

PubMed 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.

PubMed: 26543159
DOI: 10.1101/gad.270926.115

Experimental method

X-RAY DIFFRACTION (1.5 Å)