User:Khadar Abdi/Sandbox1

spinqualitylabelsall models Staphylococcus aureus threonyl-tRNA Synthetase bound to Threonyl-Sulfamoyl Adenosine Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Contents 1 General Function/Mechanism 2 Structural highlights 3 Evolutionary related proteins 4 List to available structures 5 References

General 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 TARS 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. The image to the right displays the binding of adenylate product to the TARS enzyme (PDB entry 1nyq). This is then follow up by a transferring Thr from Adenosine monophosphate molecule to 3'OH site of tRNA-thr. ^[2] The image below demonstrates the arrow pushing occurring to generate threonine bound tRNA-thr.

Lately the aaRS family was found to have more function than just aminoacylation. For instance, many aaRs molecules have been found to link with angiogenesis, blood vessel growth occuring within a cancer environment ^[4]. This is seen in human exogenous TARS in its ability to generate blood vessels within ovarian cancer environment ^[5]. Studies on the structure of TARS bound to BC194, derivative to the natural antibiotic Borrelidin, were investigated to understand how the angiogenic signaling from TARS occurs.

Structural highlights

Evolutionary 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. ↑ Mirando AC, Francklyn CS, Lounsbury KM. Regulation of angiogenesis by aminoacyl-tRNA synthetases. Int J Mol Sci. 2014 Dec 19;15(12):23725-48. doi: 10.3390/ijms151223725. PMID:25535072 doi:http://dx.doi.org/10.3390/ijms151223725
5. ↑ Mirando AC, Abdi K, Wo P, Lounsbury KM. Assessing the effects of threonyl-tRNA synthetase on angiogenesis-related responses. Methods. 2016 Nov 12. pii: S1046-2023(16)30443-1. doi:, 10.1016/j.ymeth.2016.11.007. PMID:27847344 doi:http://dx.doi.org/10.1016/j.ymeth.2016.11.007

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