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== Structural Overview ==
== Structural Overview ==
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The major structural elements of ValRS, like other class-Ia aminoacyl-tRNA synthetases, are a helical insertion into the N-terminal half of a Rossmann fold domain and an α-helix bundle domain near the C-terminus<ref>DOI 10.1261/rna.2760703</ref>. Additionally, ValRS has a large editing domain important in the discrimination between valine and structurally similar amino acids. A positively charged <scene name='10/1078173/Stem-contact-fold_domain/1'>Text To Be Displayed</scene> (SC-fold) domain contacts C11 and C25 of the D-loop of tRNA(val), creating a space between the anticodon recognition and editing domains where the tRNA is "pinched" and held onto.
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The major structural elements of ValRS, like other class-Ia aminoacyl-tRNA synthetases, are a helical insertion into the N-terminal half of a Rossmann fold domain and an α-helix bundle domain near the C-terminus<ref>DOI 10.1261/rna.2760703</ref>. Additionally, ValRS has a large editing domain important in the discrimination between valine and structurally similar amino acids. A positively charged <scene name='10/1078173/Stem-contact-fold_domain/1'>stem-contact-fold</scene> (SC-fold) domain contacts C11 and C25 of the D-loop of tRNA(val), creating a space between the anticodon recognition and editing domains where the tRNA is "pinched" and held onto.

Revision as of 22:02, 20 April 2025

Valyl-tRNA Synthetase

Valyl-tRNA synthetase (ValRS, also known as valine tRNA ligase) is the enzyme responsible for charging tRNA(val) with valine. In humans, ValRS exists in a cytosolic and a mitochondrial form. The cytosolic form is a monomeric 140kDa protein encoded by VARS1 while the mitochondrial form is a slightly smaller monomeric 118kDa protein encoded by VARS2. ValRS is a member of the class-Ia subfamily of aminoacyl-tRNA synthetases, defined by a characteristic α helix bundle at the C-terminus used for tRNA recognition. Aminoacyl-tRNA synthetases are generally highly conserved, and ValRS exhibits high structural similarity to IleRS and LeuRS. Human disease related to mutations in ValRS are very rare but life-threatening. Biallelic mutations in ValRS are associated with neurological defects and global developmental delay, including epileptic encephalopathy, microcephaly and microphthalmia[1]. These phenotypes are thought to be due to a global lack of charged tRNA molecules which induces an amino acid starvation response and inhibits cell proliferation[2].

Caption for this structure

Drag the structure with the mouse to rotate

References

  1. ↑ doi: https://dx.doi.org/doi.org/10.1038/s41467-018-07067-3
  2. ↑ doi: https://dx.doi.org/doi.org/10.3389/fcell.2019.00067
  3. ↑ 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
  4. ↑ 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
  5. ↑ doi: https://dx.doi.org/10.1261/rna.2760703

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Harry Gritsch

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