期刊
EMBO JOURNAL
卷 19, 期 14, 页码 3509-3519出版社
OXFORD UNIV PRESS
DOI: 10.1093/emboj/19.14.3509
关键词
AdoMet-dependent methyltransferase; PRMT dimer; PRMT3; protein arginine methylation; xenon derivatization
资金
- NIGMS NIH HHS [R01 GM061355, GM61355] Funding Source: Medline
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 AdoIIcy, determined at 2.0 Angstrom 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.
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