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Aminoacyl tRNA Synthetase

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'''Aminoacyl tRNA synthetase''' (aaRS) catalyzes the esterification of a specific amino acid to its cognate tRNA to form an aminoacyl-tRNA. The amino acid is transferred by the ribosome from the aminoacylated-tRNA onto a growing polypeptide chain. Class I of aaRS is a monomer or dimer, it has 2 highly conserved sequence motifs and it aminoacylates at the 2’-OH of an adenosine nucleotide. Class II of aaRS is a dimer or tetramer, it has 3 highly conserved sequence motifs and it aminoacylates at the 3’-OH of an adenosine nucleotide. CP1 domain of RS edits a mischarged aa-tRNA. Some of the crystal structures are complexes of the RS with their reactant analog: amino acid-sulfamoyl adenine (aa-SA).
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'''Aminoacyl tRNA synthetase''' (aaRS) catalyzes the esterification of a specific amino acid to its cognate tRNA to form an aminoacyl-tRNA. The amino acid is transferred by the ribosome from the aminoacylated-tRNA onto a growing polypeptide chain. Class I of aaRS is a monomer or dimer, it has 2 highly conserved sequence motifs and it aminoacylates at the 2’-OH of an adenosine nucleotide. Class II of aaRS is a dimer or tetramer, it has 3 highly conserved sequence motifs and it aminoacylates at the 3’-OH of an adenosine nucleotide. CP1 domain of RS edits a mischarged aa-tRNA. Some of the crystal structures are complexes of the RS with their reactant analog: amino acid-sulfamoyl adenine (aa-SA). For '''pyrrolysyl-RS''' details see [[Pyrrolysyl-tRNA synthetase]].
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**[[1h4q]] - TtProRS + Pro-tRNA + Pro-ol<br />
**[[1h4q]] - TtProRS + Pro-tRNA + Pro-ol<br />
**[[1h4s]] - TtProRS + Pro-tRNA + Pro-SA<br />
**[[1h4s]] - TtProRS + Pro-tRNA + Pro-SA<br />
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*'''Pyrrolysyl-RS'''
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**[[2e3c]] - MmPylRS catalytic domain <br />
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**[[3vqw]], [[3vqx]], [[4cs2]] - MmPylRS catalytic domain (mutant)<br />
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**[[3dsq]] – DhPylRS <br />
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*''Pyrrolysyl-RS binary complex''
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**[[3qtc]] – MmPylRS catalytic domain (mutant) + AMP-ATP analog<br />
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**[[2q7e]] - MmPylRS catalytic domain + ATP analog<br />
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**[[2zcd]] - MmPylRS catalytic domain + AMP-ATP analog<br />
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**[[3vqv]] - MmPylRS catalytic domain + AMPPNP <br />
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**[[2zni]] – DhPylRS + tRNA <br />
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**[[4ch3]], [[4ch4]], [[4ch5]], [[4ch6]] - MmPylRS catalytic domain + adenylated lysine derivative<br />
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**[[4cs3]] - MmPylRS catalytic domain (mutant) + adenylated lysine derivative<br />
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*''Pyrrolysyl-RS ternary complex''
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**[[2zce]] - MmPylRS catalytic domain + pyrrolysine + ATP analog<br />
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**[[2q7g]] - MmPylRS catalytic domain + pyrrolysine analog + ATP<br />
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**[[2zim]], [[2q7h]] - MmPylRS catalytic domain + adenylated pyrrolysine + pyrophosphate<br />
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**[[2zio]] - MmPylRS catalytic domain + AlocLys-AMP + ATP analog<br />
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**[[3vqy]] - MmPylRS catalytic domain + butoxycarbonyl lysine + AMPPNP <br />
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**[[4q6g]] - MmPylRS catalytic domain + acetyl lysine + ADPNP <br />
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**[[4tqd]] - MmPylRS catalytic domain + iodo-Phe + ATP <br />
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**[[4tqf]] - MmPylRS catalytic domain + bromothienylo-Ala + ATP <br />
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**[[2zin]] - MmPylRS catalytic domain + butoxycarbonyl lysine + ATP analog <br />
*'''Ser-RS'''
*'''Ser-RS'''

Revision as of 10:58, 25 May 2015

Image:3l4g.png
Crystal Structure of Aminoacyl tRNA synthetase 3l4g

Template:STRUCTURE 1f7v














Aminoacyl tRNA synthetase (aaRS) catalyzes the esterification of a specific amino acid to its cognate tRNA to form an aminoacyl-tRNA. The amino acid is transferred by the ribosome from the aminoacylated-tRNA onto a growing polypeptide chain. Class I of aaRS is a monomer or dimer, it has 2 highly conserved sequence motifs and it aminoacylates at the 2’-OH of an adenosine nucleotide. Class II of aaRS is a dimer or tetramer, it has 3 highly conserved sequence motifs and it aminoacylates at the 3’-OH of an adenosine nucleotide. CP1 domain of RS edits a mischarged aa-tRNA. Some of the crystal structures are complexes of the RS with their reactant analog: amino acid-sulfamoyl adenine (aa-SA). For pyrrolysyl-RS details see Pyrrolysyl-tRNA synthetase.


3D Structures of Aminoacyl tRNA synthetase

Updated on 25-May-2015

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Joel L. Sussman, Ann Taylor

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