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== Disease ==
== Disease ==
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A mutation in the LysS has shown to have played a role in the reduction of the outer membrane vesiculation. <ref>PMID:10592181</ref> The LysS gene has been determined to coincide with the HerC gene.
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A mutation in the LysS has shown to have played a role in the reduction of the outer membrane vesiculation. <ref>PMID:10592181</ref>
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== Relevance ==
== Relevance ==
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A defect in the translation of the genetic material from LysS would impact the functionality of the protein.
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A defect in the translation of the genetic material from LysS would impact the functionality of the protein. The LysS gene has been determined to coincide with the HerC gene. Lysyl-tRNA synthase has been thought to be used for a drug target that lead to drug discovery capable of clearing parasites from mouse models with malaria and cryptosporidiosis infection. <ref>PMID:1814685116</ref>
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== Structural highlights ==
== Structural highlights ==
The first interaction that leads to a reorganization of the active site is from the binding of the α amino group from the lysine and the carbonyl oxygen of Gly216. The second interaction is between the carboxylate group and the side chin of Arg262. The interactions of <scene name='82/824628/Lys/1'>lysine bound to gly216 and arg262</scene> both lead to the
The first interaction that leads to a reorganization of the active site is from the binding of the α amino group from the lysine and the carbonyl oxygen of Gly216. The second interaction is between the carboxylate group and the side chin of Arg262. The interactions of <scene name='82/824628/Lys/1'>lysine bound to gly216 and arg262</scene> both lead to the
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<scene name='82/824628/Reorganization/1'>reorganization of active site</scene>. When reorganizing the active sites, the ordering of two loops (residues 215-217 and 444-455) are formed. The change in the conformation of residues 393-409 is another result from the reorganization. The final change is the rotation of a 4-helix bundle (located between motif 2 & 3) by 10°. The results of these interactions is the closing up of active site upon lysine binding.
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<scene name='82/824628/Reorganization/1'>reorganization of active site</scene>. When reorganizing the active sites, the ordering of two loops (residues 215-217 and 444-455) are formed. The change in the conformation of residues 393-409 is another result from the reorganization. The final change is the rotation of a 4-helix bundle (located between motif 2 & 3) by 10°. The results of these interactions is the closing up of active site upon lysine binding.<ref>PMID:11041850</ref>
</StructureSection>
</StructureSection>
== References ==
== References ==
<references/>
<references/>

Revision as of 03:30, 30 November 2019

This Sandbox is Reserved from September 14, 2021, through May 31, 2022, for use in the class Introduction to Biochemistry taught by User:John Means at the University of Rio Grande, Rio Grande, OH, USA. This reservation includes 5 reserved sandboxes (Sandbox Reserved 1590 through Sandbox Reserved 1594).
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Lysyl-tRNA Synthetase(1BBU)

lysyl-tRNA synthetase(1BBU)

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References

  1. ↑ 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
  2. ↑ 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
  3. ↑ Onesti S, Desogus G, Brevet A, Chen J, Plateau P, Blanquet S, Brick P. Structural studies of lysyl-tRNA synthetase: conformational changes induced by substrate binding. Biochemistry. 2000 Oct 24;39(42):12853-61. PMID:11041850
  4. ↑ Ravishankar S, Ambady A, Swetha RG, Anbarasu A, Ramaiah S, Sambandamurthy VK. Essentiality Assessment of Cysteinyl and Lysyl-tRNA Synthetases of Mycobacterium smegmatis. PLoS One. 2016 Jan 21;11(1):e0147188. doi: 10.1371/journal.pone.0147188., eCollection 2016. PMID:26794499 doi:http://dx.doi.org/10.1371/journal.pone.0147188
  5. ↑ Rudd KE. EcoGene: a genome sequence database for Escherichia coli K-12. Nucleic Acids Res. 2000 Jan 1;28(1):60-4. doi: 10.1093/nar/28.1.60. PMID:10592181 doi:http://dx.doi.org/10.1093/nar/28.1.60
  6. ↑ . PMID:1814685116
  7. ↑ Onesti S, Desogus G, Brevet A, Chen J, Plateau P, Blanquet S, Brick P. Structural studies of lysyl-tRNA synthetase: conformational changes induced by substrate binding. Biochemistry. 2000 Oct 24;39(42):12853-61. PMID:11041850
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