1f3l
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CRYSTAL STRUCTURE OF THE CONSERVED CORE OF PROTEIN ARGININE METHYLTRANSFERASE PRMT3
OverviewOverview
Protein arginine methylation has been implicated in signal transduction, nuclear transport and transcription regulation. Protein arginine, methyltransferases (PRMTs) mediate the AdoMet-dependent methylation of, many proteins, including many RNA binding proteins involved in various, aspects of RNA processing and/or transport. Here we describe the crystal, structure of the rat PRMT3 catalytic core in complex with reaction product, AdoHcy, determined at 2.0 A resolution. The results reveal a two-domain, structure: an AdoMet-binding domain and a barrel-like domain. The, AdoMet-binding domain is a compact version of the consensus, AdoMet-dependent methyltransferase fold. The active site is situated in a, cone-shaped pocket between the two domains. The residues that make up the, active site are conserved across the PRMT family, consisting of a double-E, loop containing two invariant Glu and one His-Asp proton-relay system. The, structure suggests a mechanism for the methylation reaction and provides, the structural basis for functional characterization of the PRMT family., In addition, crystal packing and solution behavior suggest dimer formation, of the PRMT3 core.
About this StructureAbout this Structure
1F3L is a Single protein structure of sequence from Rattus norvegicus with SAH as ligand. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of the conserved core of protein arginine methyltransferase PRMT3., Zhang X, Zhou L, Cheng X, EMBO J. 2000 Jul 17;19(14):3509-19. PMID:10899106
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