RGD Reference Report - Crystal structure of the conserved core of protein arginine methyltransferase PRMT3. - Rat Genome Database

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Crystal structure of the conserved core of protein arginine methyltransferase PRMT3.

Authors: Zhang, X  Zhou, L  Cheng, X 
Citation: Zhang X, etal., EMBO J. 2000 Jul 17;19(14):3509-19.
RGD ID: 7243104
Pubmed: PMID:10899106   (View Abstract at PubMed)
PMCID: PMC313989   (View Article at PubMed Central)
DOI: DOI:10.1093/emboj/19.14.3509   (Journal Full-text)

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.



Gene Ontology Annotations    Click to see Annotation Detail View

Biological Process

  
Object SymbolSpeciesTermQualifierEvidenceWithNotesSourceOriginal Reference(s)
Prmt1Ratpeptidyl-arginine methylation  IDA  RGD 
Prmt3Ratpeptidyl-arginine methylation  IDA  RGD 

Molecular Function

  
Object SymbolSpeciesTermQualifierEvidenceWithNotesSourceOriginal Reference(s)
Prmt3Ratmodified amino acid binding  IDA S-Adenosyl-L-homocysteineRGD 
Prmt1Ratprotein-arginine N-methyltransferase activity  IDA  RGD 
Prmt3Ratprotein-arginine N-methyltransferase activity  IDA  RGD 

Objects Annotated

Genes (Rattus norvegicus)
Prmt1  (protein arginine methyltransferase 1)
Prmt3  (protein arginine methyltransferase 3)


Additional Information