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== General Description ==
== General Description ==
<StructureSection load='4aq7' size='340' side='right' caption='LARS (''E coli'') ternary complex with tRNA<sup>leu</sup> and leucyl adenylate analogue' scene=''>
<StructureSection load='4aq7' size='340' side='right' caption='LARS (''E coli'') ternary complex with tRNA<sup>leu</sup> and leucyl adenylate analogue' scene=''>
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Leucyl tRNA synthetase (LARS) is a 97 kDa, class I aminoacyl-tRNA synthetase (ARS) that catalyzes the ligation of leucyl adenylate with tRNA<sup>leu</sup>. LARS is a cytoplasmic enzyme that is found as part of the multisynthetase complex.
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Leucyl tRNA synthetase (LARS) is a 97 kDa, class I 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 mammals<ref>doi: 10.1007/978-3-319-46503-6_18</ref>.

Revision as of 19:39, 30 April 2018

General Description

PDB ID 4aq7

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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. 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
  3. 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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Christian Fjeld

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