A Family Divided: Distinct Structural and Mechanistic Features of the SpoU-TrmD (SPOUT) Methyltransferase Superfamily.
Catalytic Domain
Escherichia coli Proteins
/ chemistry
Methylation
Methyltransferases
/ chemistry
Models, Molecular
Protein Conformation
Protein-Arginine N-Methyltransferases
/ chemistry
S-Adenosylmethionine
/ metabolism
Saccharomyces cerevisiae Proteins
/ chemistry
Substrate Specificity
tRNA Methyltransferases
/ chemistry
Journal
Biochemistry
ISSN: 1520-4995
Titre abrégé: Biochemistry
Pays: United States
ID NLM: 0370623
Informations de publication
Date de publication:
05 02 2019
05 02 2019
Historique:
pubmed:
21
11
2018
medline:
1
10
2019
entrez:
21
11
2018
Statut:
ppublish
Résumé
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.
Identifiants
pubmed: 30457841
doi: 10.1021/acs.biochem.8b01047
pmc: PMC6541868
mid: NIHMS1027234
doi:
Substances chimiques
Escherichia coli Proteins
0
Saccharomyces cerevisiae Proteins
0
S-Adenosylmethionine
7LP2MPO46S
Methyltransferases
EC 2.1.1.-
TRM10 protein, S cerevisiae
EC 2.1.1.-
TrmD protein, E coli
EC 2.1.1.-
tRNA Methyltransferases
EC 2.1.1.-
Protein-Arginine N-Methyltransferases
EC 2.1.1.319
Sfm1 protein, S cerevisiae
EC 2.1.1.319
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Langues
eng
Sous-ensembles de citation
IM
Pagination
336-345Subventions
Organisme : NIGMS NIH HHS
ID : R01 GM130135
Pays : United States
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