Ontology highlight
ABSTRACT:
SUBMITTER: Hou YM
PROVIDER: S-EPMC6054489 | biostudies-literature | 2017
REPOSITORIES: biostudies-literature
Hou Ya-Ming YM Matsubara Ryuma R Takase Ryuichi R Masuda Isao I Sulkowska Joanna I JI
The Enzymes 20170412
TrmD is an S-adenosyl methionine (AdoMet)-dependent methyl transferase that synthesizes the methylated m<sup>1</sup>G37 in tRNA. TrmD is specific to and essential for bacterial growth, and it is fundamentally distinct from its eukaryotic and archaeal counterpart Trm5. TrmD is unusual by using a topological protein knot to bind AdoMet. Despite its restricted mobility, the TrmD knot has complex dynamics necessary to transmit the signal of AdoMet binding to promote tRNA binding and methyl transfer. ...[more]