Aminoacyl tRNA Synthetase
From Proteopedia
(Difference between revisions)
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<StructureSection load='' size='350' side='right' scene='44/444597/Cv/2' caption='Arginine tRNA synthetase complex with Arg-tRNA [[1f7v]]'> | <StructureSection load='' size='350' side='right' scene='44/444597/Cv/2' caption='Arginine tRNA synthetase complex with Arg-tRNA [[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).<ref>PMID:8422978</ref>. For '''leucine-RS''' details see [[Leucyl-tRNA Synthetase]]. For '''pyrrolysyl-RS''' details see [[Pyrrolysyl-tRNA synthetase]]. | + | '''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).<ref>PMID:8422978</ref>. For '''leucine-RS''' details see [[Leucyl-tRNA Synthetase]]. For '''pyrrolysyl-RS''' of '''pyrrolysine-tRNA ligase''' details see [[Pyrrolysyl-tRNA synthetase]]. |
</StructureSection> | </StructureSection> | ||
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**[[1irx]] – PhLysRS<br /> | **[[1irx]] – PhLysRS<br /> | ||
**[[1bbw]] – EcLysRS<br /> | **[[1bbw]] – EcLysRS<br /> | ||
| - | **[[1krs]], [[ 1krt]] – EcLysRS anticodon-binding domain – NMR<br />[[3dsq]] – DhLysRS – ''Desulfitobacterium hafniense | + | **[[1krs]], [[ 1krt]] – EcLysRS anticodon-binding domain – NMR<br /> |
| - | + | **[[3dsq]] – DhLysRS – ''Desulfitobacterium hafniense''<br /> | |
**[[3bju]] – hLysRS residues 70-579 | **[[3bju]] – hLysRS residues 70-579 | ||
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**[[3a74]] – GsLysRS + diadenosine tetraphosphate – ''Geobacillus stearothermophilus''<br /> | **[[3a74]] – GsLysRS + diadenosine tetraphosphate – ''Geobacillus stearothermophilus''<br /> | ||
**[[3e9h]], [[3e9i]] – BsLysRS + Lys-SA - ''Bacillus stearothermophilus''<br /> | **[[3e9h]], [[3e9i]] – BsLysRS + Lys-SA - ''Bacillus stearothermophilus''<br /> | ||
| - | **[[2zin]] – MmLysRS catalytic domain + Boc-Lys + ATP analog<br /> | ||
**[[1bbu]], [[1e10]], [[1lyl]] – EcLysRS + Lys<br /> | **[[1bbu]], [[1e10]], [[1lyl]] – EcLysRS + Lys<br /> | ||
**[[1e1t]] - EcLysRS + Lys-adenylate<br /> | **[[1e1t]] - EcLysRS + Lys-adenylate<br /> | ||
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| - | *'''Pyrrolysyl-RS''' | + | *'''Pyrrolysyl-RS'''; domains – RNA-binding 1-101; catalytic 188-454 |
| - | **[[2e3c]] - MmPylRS catalytic domain <br /> | + | **[[2e3c]] - MmPylRS catalytic domain - ''Methanosarcina mazei''<br /> |
**[[3vqw]], [[3vqx]], [[4cs2]] - MmPylRS catalytic domain (mutant)<br /> | **[[3vqw]], [[3vqx]], [[4cs2]] - MmPylRS catalytic domain (mutant)<br /> | ||
**[[3dsq]] – DhPylRS <br /> | **[[3dsq]] – DhPylRS <br /> | ||
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**[[2q7g]] - MmPylRS C-terminal+ pyrro-Lys analog+ ATP <br /> | **[[2q7g]] - MmPylRS C-terminal+ pyrro-Lys analog+ ATP <br /> | ||
**[[3vqv]] - MmPylRS catalytic domain + AMPPNP <br /> | **[[3vqv]] - MmPylRS catalytic domain + AMPPNP <br /> | ||
| - | **[[ | + | **[[4bw9]], [[4cs4]], [[5k1p]], [[5k1x]] - MmPylRS catalytic domain (mutant) + AMPPNP <br /> |
| + | **[[4bwa]] - MmPylRS catalytic domain (mutant) + adenylated norbornene <br /> | ||
**[[4ch3]], [[4ch4]], [[4ch5]], [[4ch6]] - MmPylRS catalytic domain + adenylated lysine derivative<br /> | **[[4ch3]], [[4ch4]], [[4ch5]], [[4ch6]] - MmPylRS catalytic domain + adenylated lysine derivative<br /> | ||
**[[4cs3]] - MmPylRS catalytic domain (mutant) + adenylated lysine derivative<br /> | **[[4cs3]] - MmPylRS catalytic domain (mutant) + adenylated lysine derivative<br /> | ||
| + | **[[5ud5]] - MmPylRS RNA-binding domain + Pyl-RNA<br /> | ||
| + | **[[5v6x]] - MmPylRS RNA-binding domain (mutant) + Pyl-RNA<br /> | ||
| + | **[[2zni]], [[2znj]] – DhPylRS + tRNA <br /> | ||
*''Pyrrolysyl-RS ternary complex'' | *''Pyrrolysyl-RS ternary complex'' | ||
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**[[4q6g]] - MmPylRS catalytic domain + acetyl lysine + ADPNP <br /> | **[[4q6g]] - MmPylRS catalytic domain + acetyl lysine + ADPNP <br /> | ||
**[[4tqd]] - MmPylRS catalytic domain + iodo-Phe + ATP <br /> | **[[4tqd]] - MmPylRS catalytic domain + iodo-Phe + ATP <br /> | ||
| - | **[[4tqf]] - MmPylRS catalytic domain + bromothienylo-Ala + ATP <br /> | + | **[[4tqf]], [[4zib]] - MmPylRS catalytic domain + bromothienylo-Ala + ATP <br /> |
**[[2zin]] - MmPylRS catalytic domain + butoxycarbonyl lysine + ATP analog <br /> | **[[2zin]] - MmPylRS catalytic domain + butoxycarbonyl lysine + ATP analog <br /> | ||
Revision as of 07:52, 30 August 2018
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3D Structures of Aminoacyl tRNA synthetase
Updated on 30-August-2018
References
- ↑ Cavarelli J, Moras D. Recognition of tRNAs by aminoacyl-tRNA synthetases. FASEB J. 1993 Jan;7(1):79-86. PMID:8422978
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Michal Harel, Alexander Berchansky, Joel L. Sussman, Ann Taylor
