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Results 1 - 10 of 20 > >>
EC Number Subunits Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 2.1.1.220? x * 29000, recombinant enzyme, SDS-PAGE, x * 28700, about, sequence calculation 736707
Display the word mapDisplay the reaction diagram Show all sequences 2.1.1.220heterodimer TRM6 and TRM61 form a compact complex via numerous hydrogen bonding and extensive hydrophobic interactions. The heterodimer interface of TRM6-TRM61 buries 3194 A2 of TRM6 and 3167 A2 of TRM61 solvent-accessible area, which represents about 17% and 16% of TRM6 and TRM61's total surface area, respectively. TRM6 mainly interacts with TRM61 through four major sites. Interaction analyses for sites A-C, detailed overview -, 758373
Display the word mapDisplay the reaction diagram Show all sequences 2.1.1.220heterotetramer dimers of tightly assembled heterodimers, formed by TrmI-6 and TrmI-61 subunits, interactions and structure analysis, overview 719192
Display the word mapDisplay the reaction diagram Show all sequences 2.1.1.220heterotetramer the eukaryotic complex of Trm6-Trm61 has been reported as a heterotetramer 756160
Display the word mapDisplay the reaction diagram Show all sequences 2.1.1.220heterotetramer the eukaryotic complex of Trm6-Trm61 has been reported as a heterotetramer. In the complex of Trm6-Trm61 from Saccharomyces cerevisiae, both subunits harbour an N-terminal domain linked to a C-terminal domain. The C-terminal domains cover a Rossmann-fold and are very similar between the two subunits, whereas significant differences are found between the N-terminal domains. The N-terminal domain of Trm61 contains a short alpha-helix and three hairpin beta-motifs, whereas Trm6 consists of a short alpha-helix with seven antiparallel beta-strands and a highly flexible region with a number of positively-charged residues. Each subunit of the Trm6-Trm61 complex forms heterodimers that, again, assemble as a heterotetramer. The catalytic subunit of this complex (Trm61) binds the cofactor SAM, a binding that is made impossible in the other subunit (Trm6) by the loss of conserved motifs involved in accommodation of this cofactor. Each heterotetramer binds two tRNA molecules onto two distal, L-shaped surfaces on the protein complex 756160
Display the word mapDisplay the reaction diagram Show all sequences 2.1.1.220heterotetramer two TRM6-TRM61 heterodimers assemble as a heterotetramer. A symmetric unit of the TRM6-TRM61 crystal contains one molecule of TRM6 and one molecule of TRM61, forming a 1:1 heterodimer. TRM6 and TRM61 form a 2:2 tetrameric heterocomplex, displaying an omega shape. Two symmetry-related TRM6-TRM61 heterodimer come together to form a central beta-barrel structure that consists of beta13 (TRM6), loop beta13/beta14 (TRM6), beta12(TRM61) and loop beta13/beta14 (TRM61). The top of the barrel contains a hydrophobic core, formed by residues Tyr422 (TRM6), Pro431 (TRM6), Met253 (TRM61), His354 (TRM61), and Tyr357 (TRM61) The center of the barrel is filled with numerous hydrophilic side-chains, including residues Glu416 (TRM6), Arg418 (TRM6), Arg420 (TRM6), Glu255 (TRM61), Gln257 (TRM61) and Arg259 (TRM61). The bottom of the barrel consists of a cage of four tyrosine residues. Modelling of the heterotetramer interface of TRM6-TRM61, overview. A TRM6-TRM61 heterotetramer constitutes two L-shaped tRNA binding regions. Structure comparison to the enzyme from Homo sapiens -, 758373
Display the word mapDisplay the reaction diagram Show all sequences 2.1.1.220homotetramer 4 * 31000, SDS-PAGE 660027
Display the word mapDisplay the reaction diagram Show all sequences 2.1.1.220homotetramer bacterial and archaeal TrmI proteins have been shown to form homotetramers. Each homotetramers accomodates up to two tRNA molecules 756160
Display the word mapDisplay the reaction diagram Show all sequences 2.1.1.220More comparative structural analysis of TrmIs, overview 719192
Display the word mapDisplay the reaction diagram Show all sequences 2.1.1.220More Gcd10p and Gcd14p function directly in m1A formation in yeast tRNAs. Purified Gcd14p alone had no enzymatic activity and is defective for tRNA binding compared with the Gcd14pyGcd10p complex. Gcd10p is required for tight binding of the tRNA substrate 485272
Results 1 - 10 of 20 > >>