1F3L

CRYSTAL STRUCTURE OF THE CONSERVED CORE OF PROTEIN ARGININE METHYLTRANSFERASE PRMT3

Summary for 1F3L

• Entry DOI: 10.2210/pdb1f3l/pdb
• Descriptor: PROTEIN ARGININE METHYLTRANSFERASE PRMT3, S-ADENOSYL-L-HOMOCYSTEINE (3 entities in total)
• Functional Keywords: beta barrel, rossmann fold, arginine methyltransferase, transferase
• Biological source: Rattus norvegicus (Norway rat)
• Cellular location: Cytoplasm: O70467
• Total number of polymer chains: 1
• Total formula weight: 36593.03

Authors

Zhang, X.,Zhou, L.,Cheng, X. (deposition date: 2000-06-05, release date: 2001-03-14, Last modification date: 2024-02-07)

Primary citation

Zhang, X.,Zhou, L.,Cheng, X.
Crystal structure of the conserved core of protein arginine methyltransferase PRMT3.
EMBO J., 19:3509-3519, 2000

PubMed Abstract: 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.

PubMed: 10899106
DOI: 10.1093/emboj/19.14.3509

Experimental method

X-RAY DIFFRACTION (2.03 Å)