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- W2900599151 abstract "The SPOUT family of enzymes makes up the second largest of seven structurally distinct groups of methyltransferases and is named after two evolutionarily related RNA methyltransferases, SpoU and TrmD. A deep trefoil knotted domain in the tertiary structures of member enzymes defines the SPOUT family. For many years, formation of a homodimeric quaternary structure was thought to be a strict requirement for all SPOUT enzymes, critical for substrate binding and formation of the active site. However, recent structural characterization of two SPOUT members, Trm10 and Sfm1, revealed that they function as monomers without the requirement of this critical dimerization. This unusual monomeric form implies that these enzymes must exhibit a nontraditional substrate binding mode and active site architecture and may represent a new division in the SPOUT family with distinct properties removed from the dimeric enzymes. Here we discuss the mechanistic features of SPOUT enzymes with an emphasis on the monomeric members and implications of this “novel” monomeric structure on cofactor and substrate binding." @default.
- W2900599151 created "2018-11-29" @default.
- W2900599151 creator A5002863056 @default.
- W2900599151 creator A5022205141 @default.
- W2900599151 date "2018-11-20" @default.
- W2900599151 modified "2023-10-14" @default.
- W2900599151 title "A Family Divided: Distinct Structural and Mechanistic Features of the SpoU-TrmD (SPOUT) Methyltransferase Superfamily" @default.
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- W2900599151 doi "https://doi.org/10.1021/acs.biochem.8b01047" @default.
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- W2900599151 hasPublicationYear "2018" @default.
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