Application | Comment | Organism |
---|---|---|
drug development | TrmD is a leading antimicrobial drug target, due to its essentiality for bacterial growth, its broad conservation across bacterial species, and its deep-rooted distinction from the human and archaeal counterpart Trm5, which has the dinucleotide fold | Haemophilus influenzae |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
sinefungin | - |
Haemophilus influenzae |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | Haemophilus influenzae | TrmD is a bacterial enzyme with a trefoil-knot in the active site, involving three crossings of the protein backbone through a loop. TrmD catalyzes methyl transfer from AdoMet to the N1 of G37 on the 3' side of the tRNA anticodon | ? | - |
- |
|
S-adenosyl-L-methionine + guanine37 in tRNA | Haemophilus influenzae | - |
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Haemophilus influenzae | A0A0D0GZF5 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | TrmD is a bacterial enzyme with a trefoil-knot in the active site, involving three crossings of the protein backbone through a loop. TrmD catalyzes methyl transfer from AdoMet to the N1 of G37 on the 3' side of the tRNA anticodon | Haemophilus influenzae | ? | - |
- |
|
S-adenosyl-L-methionine + guanine37 in tRNA | - |
Haemophilus influenzae | S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | enzyme structures of apo- and binary tRNA-free forms, and of ternary complex including AdoMet, molecular dynamic analysis, simulations and modelling, overview. Molecular mechanics Poisson-Boltzmann surface area (MMPBSA) method | Haemophilus influenzae |
Synonyms | Comment | Organism |
---|---|---|
TrmD | - |
Haemophilus influenzae |
tRNA(m(1)G37)methyltransferase | - |
Haemophilus influenzae |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
S-adenosyl-L-methionine | - |
Haemophilus influenzae |
General Information | Comment | Organism |
---|---|---|
evolution | the TrmD knot is closely related to the trefoil-knot in SpoU methyl transferases, which catalyze 2'-O-methylation to RNA ribose for wide-ranging activities. In virtually all aspects of the methyl transfer reaction, TrmD is distinct from related Trm5 | Haemophilus influenzae |
malfunction | elimination of TrmD increases protein synthesis frameshifts and causes cell death | Haemophilus influenzae |
additional information | the structurally constrained TrmD knot is required for its catalytic activity. The TrmD knot has complex internal movements that respond to AdoMet binding and signaling. Most of the signaling propagates the free energy of AdoMet binding to stabilize tRNA binding and to assemble the active site. Principles of knots as an organized structure that captures the free energies of substrate binding to facilitate catalysis, overview | Haemophilus influenzae |
physiological function | in bacteria, TrmD is a methyl transferase that uses a knotted protein fold to catalyze methyl transfer from S-adenosyl methionine (AdoMet) to G37-tRNA. The product m1G37-tRNA is essential for life as a determinant to maintain protein synthesis reading-frame | Haemophilus influenzae |