2003
DOI: 10.1016/j.jmb.2003.09.011
|View full text |Cite
|
Sign up to set email alerts
|

Insights into Catalysis by a Knotted TrmD tRNA Methyltransferase

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
2
1
1
1

Citation Types

13
211
0

Year Published

2006
2006
2020
2020

Publication Types

Select...
8

Relationship

0
8

Authors

Journals

citations
Cited by 118 publications
(224 citation statements)
references
References 31 publications
13
211
0
Order By: Relevance
“…While different in spatial configuration, each network is elaborate and comprehensive in the stabilization of the N 1 , N 6 , and N 7 of the adenine ring, the 29-and 39-OH of the ribose, and the carboxyl and amino groups of methionine in the methyl donor. These stabilizing forces are well visualized in a binary structure of TrmD with AdoMet and are preserved in a product complex with S-adenosyl homocysteine (AdoHcy) (Ahn et al 2003;Elkins et al 2003). They are also clearly identified in a binary structure of Trm5 with sinefungin and in a ternary structure with AdoMet and tRNA (Goto-Ito et al 2008).…”
Section: Introductionmentioning
confidence: 85%
See 1 more Smart Citation
“…While different in spatial configuration, each network is elaborate and comprehensive in the stabilization of the N 1 , N 6 , and N 7 of the adenine ring, the 29-and 39-OH of the ribose, and the carboxyl and amino groups of methionine in the methyl donor. These stabilizing forces are well visualized in a binary structure of TrmD with AdoMet and are preserved in a product complex with S-adenosyl homocysteine (AdoHcy) (Ahn et al 2003;Elkins et al 2003). They are also clearly identified in a binary structure of Trm5 with sinefungin and in a ternary structure with AdoMet and tRNA (Goto-Ito et al 2008).…”
Section: Introductionmentioning
confidence: 85%
“…While both enzymes recognize AdoMet as the methyl donor and G37-tRNA as the acceptor, they share no structural homology. TrmD functions as a homodimer and binds AdoMet using a rare trefoilknot fold (Ahn et al 2003;Elkins et al 2003), whereas Trm5 functions as a monomer and binds AdoMet using the popular protein fold known as the Rossmann fold (Goto-Ito et al 2008. Importantly, crystal structures of these enzymes show that the AdoMet structure when bound to TrmD exists in an L-shaped bent conformation (Ahn et al 2003), where the methionine moiety bends over the adenosine moiety, whereas the AdoMet structure when bound to Trm5 exists in an extended open conformation (Fig.…”
Section: Introductionmentioning
confidence: 99%
“…41 In the case of m 1 G RNA methyltransferase (TrmD), 41 an aspartate residue was shown to be involved in the deprotonation step of N 1 of guanine. The two processes are likely to be different, as under physiological conditions, the N 1 of guanine is protonated but that of adenine is not.…”
Section: Superimposition Of T Thermophilus and M Tuberculosismentioning
confidence: 99%
“…5). Structurally equivalent arginine is also conserved in TrmD (R154 in E. coli) and is shown to be part of its catalytic center (Elkins et al 2003). The role of highly conserved arginine in the catalytic center of another SPOUT (Watanabe et al 2005).…”
Section: Ybea Protein Has C1915-specific Methyltransferase Activity Imentioning
confidence: 99%