Structural comparison of tRNA m1A58 methyltransferases revealed different molecular strategies to maintain their oligomeric architecture under extreme conditions

Table 1 Crystal structures of TrmI proteins available in the PDB.

Name	Species (domain of life)	Optimal growth temperature ^a (°C)	PDB code	Resolution (Å)	Space group	ligand	Number of monomers in the asymmetric unit^b
_HsTrmI-61	H. sapiens (E)	37 (M)	2B25	2.5	C222₁	SAM	2
_MtTrmI	M. tuberculosis (B)	37 (M)	1I9G	1.98	I222	SAM	1
_TtTrmI	T. thermophilus (B)	70 (T)	2PWY	1.7	C222₁	SAH	2
_TmTrmI	T. maritima (B)	77-80 (T/HT)	1O54	1.65	I222	-	1
_AaTrmI	A. aeolicus (B)	85-96 (HT)	2YVL	2.2	P2₁2₁2₁	SAM	4
_PaTrmI	P. abyssi (A)	100-103 (HT, Ba)	3LHD 3LGA 3MB5	2.6 2.05 1.6	P2₁2₁2₁ P3₁ I222	SAH SAH SAM	4 4 1

^a When different optimal growth temperatures have been reported, a range of temperature is given.
^b The biological assembly predicted by PISA is a tetramer in all cases.
A: Archaea, B: Bacteria, E: Eukarya
Ba: Barophile, M: Mesophile, T: Thermophile, HT: Hyperthermophile
SAM: S-adenosyl-L-methionine
SAH: S-adenosyl-L-homocysteine

ISSN: 1472-6807