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Aminoacyl tRNA Synthetase
From Proteopedia
(Difference between revisions)
| Line 38: | Line 38: | ||
*'''Class I aaRS''' | *'''Class I aaRS''' | ||
| - | *Arg-RS | + | *'''Arg-RS''' |
**[[1bs2]] – yArgRS<br /> | **[[1bs2]] – yArgRS<br /> | ||
| Line 54: | Line 54: | ||
**[[2zue]] – PhArgRS + Arg-tRNA + ATP analog | **[[2zue]] – PhArgRS + Arg-tRNA + ATP analog | ||
| - | *Cys-RS | + | *'''Cys-RS''' |
**[[1li5]] - EcCysRS - ''Escherichia coli''<br /> | **[[1li5]] - EcCysRS - ''Escherichia coli''<br /> | ||
| Line 60: | Line 60: | ||
**[[1u0b]] – EcCysRS + Cys-tRNA | **[[1u0b]] – EcCysRS + Cys-tRNA | ||
| - | *Gln-RS | + | *'''Gln-RS''' |
**[[1nyl]]– EcGlnRS<br /> | **[[1nyl]]– EcGlnRS<br /> | ||
| Line 74: | Line 74: | ||
**[[1exd]] - EcGlnRS + Gln-tRNA (mutant) + AMP | **[[1exd]] - EcGlnRS + Gln-tRNA (mutant) + AMP | ||
| - | *Glu-RS | + | *'''Glu-RS''' |
**[[1gln]] – TtGluRS<br /> | **[[1gln]] – TtGluRS<br /> | ||
| Line 106: | Line 106: | ||
**[[2hrk]], [[ 2hsm]] - yGluRS N-terminal + GU4 nucleic-binding protein 1 | **[[2hrk]], [[ 2hsm]] - yGluRS N-terminal + GU4 nucleic-binding protein 1 | ||
| - | *Ile-RS | + | *'''Ile-RS''' |
**[[1ile]] - TtIleRS<br /> | **[[1ile]] - TtIleRS<br /> | ||
| Line 123: | Line 123: | ||
**[[1ffy]], [[ 1qu2]], [[ 1qu3]] - SaIleRS + Ile-tRNA + antibiotic - ''Staphylococcus aureus'' | **[[1ffy]], [[ 1qu2]], [[ 1qu3]] - SaIleRS + Ile-tRNA + antibiotic - ''Staphylococcus aureus'' | ||
| - | *Leu-RS | + | *'''Leu-RS''' |
**[[3o0a]] – AaLeuRS hydrolytic domain – ''Aquifex aeolicus''<br />[[2wfd]] – hLeuRS editing domain – human<br /> | **[[3o0a]] – AaLeuRS hydrolytic domain – ''Aquifex aeolicus''<br />[[2wfd]] – hLeuRS editing domain – human<br /> | ||
| Line 146: | Line 146: | ||
**[[2bte]], [[ 2byt]] - TtLeuRS + Leu-tRNA + Leu | **[[2bte]], [[ 2byt]] - TtLeuRS + Leu-tRNA + Leu | ||
| - | *Lys-RS | + | *'''Lys-RS''' |
**[[1irx]] – PhLysRS<br /> | **[[1irx]] – PhLysRS<br /> | ||
| Line 170: | Line 170: | ||
**[[1e24]] - EcLysRS + Lys + ATP | **[[1e24]] - EcLysRS + Lys + ATP | ||
| - | *'' | + | *''Lys-RS + tRNA''<br /> |
**[[2zni]], [[2znj]] – DhLysRS + tRNA | **[[2zni]], [[2znj]] – DhLysRS + tRNA | ||
| - | *Met-RS | + | *'''Met-RS''' |
**[[1a8h]] – TtMetRS<br /> | **[[1a8h]] – TtMetRS<br /> | ||
| Line 213: | Line 213: | ||
**[[2hsn]] - yMetRS N-terminal + GU4 nucleic-binding protein 1 N-terminal | **[[2hsn]] - yMetRS N-terminal + GU4 nucleic-binding protein 1 N-terminal | ||
| - | *Trp-RS | + | *'''Trp-RS''' |
**[[1d2r]] - GsTrpRS<br /> | **[[1d2r]] - GsTrpRS<br /> | ||
| Line 258: | Line 258: | ||
**[[2ake]], [[2dr2]] - hTrpRS + Trp-tRNA | **[[2ake]], [[2dr2]] - hTrpRS + Trp-tRNA | ||
| - | *Tyr-RS | + | *'''Tyr-RS''' |
**[[1tya]], [[ 1tyb]], [[ 1tyc]], [[ 1tyd]], [[ 2ts1]] – GsTyrRS<br /> | **[[1tya]], [[ 1tyb]], [[ 1tyc]], [[ 1tyd]], [[ 2ts1]] – GsTyrRS<br /> | ||
| Line 303: | Line 303: | ||
**[[2rkj]] – NcTyrRS + RNA | **[[2rkj]] – NcTyrRS + RNA | ||
| - | *Val-RS | + | *'''Val-RS''' |
**[[1iyw]] - TtValRS<br /> | **[[1iyw]] - TtValRS<br /> | ||
| Line 315: | Line 315: | ||
*'''Class II aaRS''' | *'''Class II aaRS''' | ||
| - | *Ala-RS | + | *'''Ala-RS''' |
**[[3g98]] – AaAlaRS residues 758-867<br /> | **[[3g98]] – AaAlaRS residues 758-867<br /> | ||
| Line 335: | Line 335: | ||
**[[2ztg]] – AfAlaRS + Ala-SA<br /> | **[[2ztg]] – AfAlaRS + Ala-SA<br /> | ||
| - | *Asp-RS | + | *'''Asp-RS''' |
**[[3nen]], [[1b8a]] – TkAspRS - ''Thermococcus kodakarensis''<br /> | **[[3nen]], [[1b8a]] – TkAspRS - ''Thermococcus kodakarensis''<br /> | ||
| Line 341: | Line 341: | ||
**[[1wyd]] – AspRS – ''Sulfolobus tokodaii''<br /> | **[[1wyd]] – AspRS – ''Sulfolobus tokodaii''<br /> | ||
**[[1eov]] - yAspRS<br /> | **[[1eov]] - yAspRS<br /> | ||
| - | [[1n9w]], [[1l0w]], [[1g51]] – TtAspRS<br /> | + | **[[1n9w]], [[1l0w]], [[1g51]] – TtAspRS<br /> |
**[[1eqr]] – EcAspRS | **[[1eqr]] – EcAspRS | ||
| Line 358: | Line 358: | ||
**[[1il2]], [[1c0a]] – EcAspRS + Asp-tRNA + Asp-adenylate | **[[1il2]], [[1c0a]] – EcAspRS + Asp-tRNA + Asp-adenylate | ||
| - | *Asn-RS | + | *'''Asn-RS''' |
**[[1x56]] - PhAsnRS <br /> | **[[1x56]] - PhAsnRS <br /> | ||
| Line 372: | Line 372: | ||
**[[12as]] - EcAsnRS + Asn + AMP | **[[12as]] - EcAsnRS + Asn + AMP | ||
| - | *Gly-RS | + | *'''Gly-RS''' |
**[[1ati]] – TtGlyRS<br /> | **[[1ati]] – TtGlyRS<br /> | ||
| Line 390: | Line 390: | ||
**[[1ggm]] – TtGlyRS + Gly-adenylate | **[[1ggm]] – TtGlyRS + Gly-adenylate | ||
| - | *His-RS | + | *'''His-RS''' |
**[[3net]] – HisRS – Nostoc<br /> | **[[3net]] – HisRS – Nostoc<br /> | ||
| Line 407: | Line 407: | ||
**[[1kmn]] - EcHisRS + His-ol + ATP | **[[1kmn]] - EcHisRS + His-ol + ATP | ||
| - | *Phe-RS | + | *'''Phe-RS''' |
**[[1pys]] – TtPheRS<br /> | **[[1pys]] – TtPheRS<br /> | ||
| Line 430: | Line 430: | ||
**[[2iy5]] - TtPheRS α+β chains + Phe-ol + Phe-tRNA | **[[2iy5]] - TtPheRS α+β chains + Phe-ol + Phe-tRNA | ||
| - | *Pro-RS | + | *'''Pro-RS''' |
**[[1hc7]] – TtProRS<br /> | **[[1hc7]] – TtProRS<br /> | ||
| Line 452: | Line 452: | ||
**[[1h4s]] - TtProRS + Pro-tRNA + Pro-SA<br /> | **[[1h4s]] - TtProRS + Pro-tRNA + Pro-SA<br /> | ||
| - | *Ser-RS | + | *'''Ser-RS''' |
**[[3lsq]] – TbSerRS<br /> | **[[3lsq]] – TbSerRS<br /> | ||
| Line 483: | Line 483: | ||
**[[2du5]], [[2du6]] - AfSerRS (mutant) + Cys-tRNA + phosphoserine | **[[2du5]], [[2du6]] - AfSerRS (mutant) + Cys-tRNA + phosphoserine | ||
| - | *Thr-RS | + | *'''Thr-RS''' |
**[[1y2q]] - PaThrRS editing domain<br /> | **[[1y2q]] - PaThrRS editing domain<br /> | ||
Revision as of 12:04, 16 November 2014
Image:3l4g.png
Crystal Structure of Aminoacyl tRNA synthetase 3l4g
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).
3D Structures of Aminoacyl tRNA synthetase
Updated on 16-November-2014
Proteopedia Page Contributors and Editors (what is this?)
Michal Harel, Alexander Berchansky, Joel L. Sussman, Ann Taylor
