1orh
From Proteopedia
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Structure of the Predominant Protein Arginine Methyltransferase PRMT1
Overview
PRMT1 is the predominant type I protein arginine methyltransferase in, mammals and highly conserved among all eukaryotes. It is essential for, early postimplantation development in mouse. Here we describe the crystal, structure of rat PRMT1 in complex with the reaction product AdoHcy and a, 19 residue substrate peptide containing three arginines. The results, reveal a two-domain structure-an AdoMet binding domain and a barrel-like, domain-with the active site pocket located between the two domains., Mutagenesis studies confirmed that two active site glutamates are, essential for enzymatic activity, and that dimerization of PRMT1 is, essential for AdoMet binding. Three peptide binding channels are, identified: two are between the two domains, and the third is on the, surface perpendicular to the strands forming the beta barrel.
About this Structure
1ORH is a Single protein structure of sequence from Rattus norvegicus with SAH and GOL as ligands. Active as Histone-arginine N-methyltransferase, with EC number 2.1.1.125 Full crystallographic information is available from OCA.
Reference
Structure of the predominant protein arginine methyltransferase PRMT1 and analysis of its binding to substrate peptides., Zhang X, Cheng X, Structure. 2003 May;11(5):509-20. PMID:12737817
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