1F3L

CRYSTAL STRUCTURE OF THE CONSERVED CORE OF PROTEIN ARGININE METHYLTRANSFERASE PRMT3

1F3L の概要

• エントリーDOI: 10.2210/pdb1f3l/pdb
• 分子名称: PROTEIN ARGININE METHYLTRANSFERASE PRMT3, S-ADENOSYL-L-HOMOCYSTEINE (3 entities in total)
• 機能のキーワード: beta barrel, rossmann fold, arginine methyltransferase, transferase
• 由来する生物種: Rattus norvegicus (Norway rat)
• 細胞内の位置: Cytoplasm: O70467
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 36593.03

構造登録者

Zhang, X.,Zhou, L.,Cheng, X. (登録日: 2000-06-05, 公開日: 2001-03-14, 最終更新日: 2024-02-07)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.03 Å)