User:Khadar Abdi/Sandbox1

spinqualitylabelsall models Human Threonyl tRNA Synthetase bound to L-threoninamide Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Contents 1 Function/Mechanism 2 Structural highlights 3 Structural insight into Aminoacylation 4 Evolutionarily related proteins 5 List to available structures 6 References

Function/Mechanism

Threonyl t-RNA Synthetase or Threonyl-tRNA ligase or TARS is class II Aminoacyl-tRNA synthetase enzymes. These enzymes primary function are to added the respective amino acid to the respective transfer Ribonucleic Acid (tRNA-AA) The main function of the enzyme is to add Threonine amino acid (Thr) to threonine specific tRNA (tRNA-thr) a necessity prep for the protein synthesis pathway. Below displays the overview of the Aminoacylation rxn ^[1]

TARS adds amino acid to tRNA by a two-step mechanism. First the enzyme binds to both and in the catalytic domain to perform an adenylation reaction in which pyrophosphate is released as a byproduct. This is then follow up by a transferring Thr from Adenosine monophosphate molecule to 3'OH site of tRNA-thr. ^[2] Image below demonstrates the arrow pushing occuring to generate threonine bound tRNA-thr.

You may include any references to papers as in: the use of JSmol in Proteopedia ^[4] or to the article describing Jmol ^[5] to the rescue.

Structural highlights

Structural insight into Aminoacylation

Evolutionarily related proteins

List to available structures

References

1. ↑ Rajendran V, Kalita P, Shukla H, Kumar A, Tripathi T. Aminoacyl-tRNA synthetases: Structure, function, and drug discovery. Int J Biol Macromol. 2018 May;111:400-414. doi: 10.1016/j.ijbiomac.2017.12.157., Epub 2018 Jan 3. PMID:29305884 doi:http://dx.doi.org/10.1016/j.ijbiomac.2017.12.157
2. ↑ Lehninger, A. L., Nelson, D. L., & Cox, M. M. (2000). Lehninger principles of biochemistry. New York: Worth Publishers.
3. ↑ Lehninger, A. L., Nelson, D. L., & Cox, M. M. (2000). Lehninger principles of biochemistry. New York: Worth Publishers.
4. ↑ 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
5. ↑ 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

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