Sandbox Reserved 1583
From Proteopedia
(Difference between revisions)
Line 7: | Line 7: | ||
== Function == | == Function == | ||
- | Lysyl-tRNA synthetase (LysS) is a member of the class II aminoacyl-tRNA synthetases and catalyses the specific aminoacylation of tRNA(Lys). There are two different proteins that code for | + | Lysyl-tRNA synthetase (LysS) is a member of the class II aminoacyl-tRNA synthetases and catalyses the specific aminoacylation of tRNA(Lys). There are two different proteins that code for lysyl-tRNA synthase, LysS and LysU. The LysS is expressed under normal contionds, where the LysU is overexpressed in conditions like high temperature, anaerobiosis, low external pH, or the presence of leucine. <ref>PMID:11041850</ref> The source organism comes from Escherichia coli. The LysS is a protein that plays an important role in the translation of the genetic sequence. The LysS aids in an accurate translation of the mRNA. <ref>PMID:26794499</ref> |
Revision as of 00:59, 30 November 2019
This Sandbox is Reserved from September 14, 2021, through May 31, 2022, for use in the class Introduction to Biochemistry taught by User:John Means at the University of Rio Grande, Rio Grande, OH, USA. This reservation includes 5 reserved sandboxes (Sandbox Reserved 1590 through Sandbox Reserved 1594). |
To get started:
More help: Help:Editing. For an example of a student Proteopedia page, please see Photosystem II, Tetanospasmin, or Guanine riboswitch. |
Lysyl-tRNA Synthetase(1BBU)
|
References
- ↑ Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
- ↑ Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644
- ↑ Onesti S, Desogus G, Brevet A, Chen J, Plateau P, Blanquet S, Brick P. Structural studies of lysyl-tRNA synthetase: conformational changes induced by substrate binding. Biochemistry. 2000 Oct 24;39(42):12853-61. PMID:11041850
- ↑ Ravishankar S, Ambady A, Swetha RG, Anbarasu A, Ramaiah S, Sambandamurthy VK. Essentiality Assessment of Cysteinyl and Lysyl-tRNA Synthetases of Mycobacterium smegmatis. PLoS One. 2016 Jan 21;11(1):e0147188. doi: 10.1371/journal.pone.0147188., eCollection 2016. PMID:26794499 doi:http://dx.doi.org/10.1371/journal.pone.0147188