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== General Description ==
== General Description ==
<StructureSection load='4aq7' frame='true' size='340' side='right' caption='LARS (E coli) ternary complex with tRNAleu and leucyl adenylate analogue' scene='78/786656/Lars/2'>
<StructureSection load='4aq7' frame='true' size='340' side='right' caption='LARS (E coli) ternary complex with tRNAleu and leucyl adenylate analogue' scene='78/786656/Lars/2'>
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Leucyl tRNA synthetase (LARS) is a 97 kDa, class IA aminoacyl-tRNA synthetase (ARS) that catalyzes the ligation of leucine with tRNA<sup>leu</sup> in an ATP dependent mechanism. LARS is a cytoplasmic enzyme that is found as part of the multisynthetase complex in eukaryotes<ref>doi: 10.1007/978-3-319-46503-6_18</ref>. The multi-synthetase complex contains glutamylprolyl-tRNA synthetase (EPRS), isoleucyl (IARS), leucyl (LARS), glutaminyl (GARS), methionyl (MARS), lysyl (KARS), arginyl (RARS), and aspartyl (DARS) tRNA synthetases as well as p18, p38 and p43<ref>doi: 10.1016/S0006-291X(03)00485-6</ref>.
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<scene name='78/786656/Total/1'>Leucyl tRNA synthetase (LARS)</scene> is a 97 kDa, class IA aminoacyl-tRNA synthetase (ARS) that catalyzes the ligation of leucine with tRNA<sup>leu</sup> in an ATP dependent mechanism. LARS is a cytoplasmic enzyme that is found as part of the multisynthetase complex in eukaryotes<ref>doi: 10.1007/978-3-319-46503-6_18</ref>. The multi-synthetase complex contains glutamylprolyl-tRNA synthetase (EPRS), isoleucyl (IARS), leucyl (LARS), glutaminyl (GARS), methionyl (MARS), lysyl (KARS), arginyl (RARS), and aspartyl (DARS) tRNA synthetases as well as p18, p38 and p43<ref>doi: 10.1016/S0006-291X(03)00485-6</ref>.
Multisynthetase complexes have also been seen in some archaea such as ''Thermococcus kodakarensis'' although the composition of the complex is not the same as eukaryotes<ref>doi: 10.1016/j.febslet.2012.05.039</ref>.
Multisynthetase complexes have also been seen in some archaea such as ''Thermococcus kodakarensis'' although the composition of the complex is not the same as eukaryotes<ref>doi: 10.1016/j.febslet.2012.05.039</ref>.
LARS has been shown to be involved with the mTOR pathways as a sensor of leucine levels within the cell<ref>doi: 10.1016/j.cell.2012.02.044</ref>.
LARS has been shown to be involved with the mTOR pathways as a sensor of leucine levels within the cell<ref>doi: 10.1016/j.cell.2012.02.044</ref>.

Revision as of 01:45, 2 May 2018

General Description

LARS (E coli) ternary complex with tRNAleu and leucyl adenylate analogue

Drag the structure with the mouse to rotate

3D Structure of LARS

Updated on 02-May-2018

References

  1. ↑ Mirande M. The Aminoacyl-tRNA Synthetase Complex. Subcell Biochem. 2017;83:505-522. doi: 10.1007/978-3-319-46503-6_18. PMID:28271488 doi:http://dx.doi.org/10.1007/978-3-319-46503-6_18
  2. ↑ Han JM, Kim JY, Kim S. Molecular network and functional implications of macromolecular tRNA synthetase complex. Biochem Biophys Res Commun. 2003 Apr 18;303(4):985-93. doi: , 10.1016/s0006-291x(03)00485-6. PMID:12684031 doi:http://dx.doi.org/10.1016/s0006-291x(03)00485-6
  3. ↑ Raina M, Elgamal S, Santangelo TJ, Ibba M. Association of a multi-synthetase complex with translating ribosomes in the archaeon Thermococcus kodakarensis. FEBS Lett. 2012 Jul 30;586(16):2232-8. doi: 10.1016/j.febslet.2012.05.039. Epub, 2012 Jun 7. PMID:22683511 doi:http://dx.doi.org/10.1016/j.febslet.2012.05.039
  4. ↑ Han JM, Jeong SJ, Park MC, Kim G, Kwon NH, Kim HK, Ha SH, Ryu SH, Kim S. Leucyl-tRNA synthetase is an intracellular leucine sensor for the mTORC1-signaling pathway. Cell. 2012 Apr 13;149(2):410-24. doi: 10.1016/j.cell.2012.02.044. Epub 2012 Mar, 15. PMID:22424946 doi:http://dx.doi.org/10.1016/j.cell.2012.02.044
  5. ↑ Pierce SB, Gersak K, Michaelson-Cohen R, Walsh T, Lee MK, Malach D, Klevit RE, King MC, Levy-Lahad E. Mutations in LARS2, encoding mitochondrial leucyl-tRNA synthetase, lead to premature ovarian failure and hearing loss in Perrault syndrome. Am J Hum Genet. 2013 Apr 4;92(4):614-20. doi: 10.1016/j.ajhg.2013.03.007. Epub, 2013 Mar 28. PMID:23541342 doi:http://dx.doi.org/10.1016/j.ajhg.2013.03.007
  6. ↑ Cusack S, Yaremchuk A, Tukalo M. The 2 A crystal structure of leucyl-tRNA synthetase and its complex with a leucyl-adenylate analogue. EMBO J. 2000 May 15;19(10):2351-61. PMID:10811626 doi:10.1093/emboj/19.10.2351
  7. ↑ Palencia A, Crepin T, Vu MT, Lincecum TL Jr, Martinis SA, Cusack S. Structural dynamics of the aminoacylation and proofreading functional cycle of bacterial leucyl-tRNA synthetase. Nat Struct Mol Biol. 2012 Jun 10. doi: 10.1038/nsmb.2317. PMID:22683997 doi:10.1038/nsmb.2317
  8. ↑ Seiradake E, Mao W, Hernandez V, Baker SJ, Plattner JJ, Alley MR, Cusack S. Crystal structures of the human and fungal cytosolic Leucyl-tRNA synthetase editing domains: A structural basis for the rational design of antifungal benzoxaboroles. J Mol Biol. 2009 Jul 10;390(2):196-207. Epub 2009 May 6. PMID:19426743 doi:10.1016/j.jmb.2009.04.073
  9. ↑ Liu Y, Liao J, Zhu B, Wang ED, Ding J. Crystal structures of the editing domain of Escherichia coli leucyl-tRNA synthetase and its complexes with Met and Ile reveal a lock-and-key mechanism for amino acid discrimination. Biochem J. 2006 Mar 1;394(Pt 2):399-407. PMID:16277600 doi:10.1042/BJ20051249

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