Sandbox Reserved 1583

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== Function ==
== Function ==
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Lysyl-tRNA synthetase (LysS) is a member of the class II aminoacyl-tRNA synthetases and catalyses the specific aminoacylation of tRNA(Lys). <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.
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Lysyl-tRNA synthetase (LysS) is a member of the class II aminoacyl-tRNA synthetases and catalyses the specific aminoacylation of tRNA(Lys). <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. LysS aids in an accurate translation of the mRNA. <ref>PMID:26794499</ref>

Revision as of 20:24, 29 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:
  • Click the edit this page tab at the top. Save the page after each step, then edit it again.
  • Click the 3D button (when editing, above the wikitext box) to insert Jmol.
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  • Add a description of your scene. Use the buttons above the wikitext box for bold, italics, links, headlines, etc.

More help: Help:Editing. For an example of a student Proteopedia page, please see Photosystem II, Tetanospasmin, or Guanine riboswitch.

Lysyl-tRNA Synthetase(1BBU)

lysyl-tRNA synthetase(1BBU)

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References

  1. ↑ 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
  2. ↑ 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
  3. ↑ 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
  4. ↑ 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
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