A substrate binding model for the KEOPS tRNA modifying complex
KEOPS is an evolutionary conserved complex with a core of four core subunits—Pcc1, Kae1, Bud32 and Cgi121—that catalyzes the universal and essential tRNA modification N6-threonylcarbamoyl adenosine (t6A). Here the authors describe a Cgi121-tRNA crystal structure and new composite model of the KEOPS...
Saved in:
Main Authors: | Jonah Beenstock, Samara Mishelle Ona, Jennifer Porat, Stephen Orlicky, Leo C. K. Wan, Derek F. Ceccarelli, Pierre Maisonneuve, Rachel K. Szilard, Zhe Yin, Dheva Setiaputra, Daniel Y. L. Mao, Morgan Khan, Shaunak Raval, David C. Schriemer, Mark A. Bayfield, Daniel Durocher, Frank Sicheri |
---|---|
Format: | article |
Language: | EN |
Published: |
Nature Portfolio
2020
|
Subjects: | |
Online Access: | https://doaj.org/article/7cf78e57b0794aac8b3b0de7021b5c2b |
Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
Similar Items
-
Chimeric design of pyrrolysyl-tRNA synthetase/tRNA pairs and canonical synthetase/tRNA pairs for genetic code expansion
by: Wenlong Ding, et al.
Published: (2020) -
Quantitative tRNA-sequencing uncovers metazoan tissue-specific tRNA regulation
by: Otis Pinkard, et al.
Published: (2020) -
Biogenesis and functions of aminocarboxypropyluridine in tRNA
by: Mayuko Takakura, et al.
Published: (2019) -
Mechanism of aminoacyl-tRNA acetylation by an aminoacyl-tRNA acetyltransferase AtaT from enterohemorrhagic E. coli
by: Yuka Yashiro, et al.
Published: (2020) -
Transforming a pair of orthogonal tRNA-aminoacyl-tRNA synthetase from Archaea to function in mammalian cells.
by: Gabrielle Nina Thibodeaux, et al.
Published: (2010)