2hl2
From Proteopedia
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|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=SSA:5'-O-(N-(L-SERYL)-SULFAMOYL)ADENOSINE'>SSA</scene> | |LIGAND= <scene name='pdbligand=SSA:5'-O-(N-(L-SERYL)-SULFAMOYL)ADENOSINE'>SSA</scene> | ||
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Threonine--tRNA_ligase Threonine--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.3 6.1.1.3] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Threonine--tRNA_ligase Threonine--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.3 6.1.1.3] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1y2q|1Y2Q]], [[2hkz|2HKZ]], [[2hl0|2HL0]], [[2hl1|2HL1]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2hl2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hl2 OCA], [http://www.ebi.ac.uk/pdbsum/2hl2 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2hl2 RCSB]</span> | ||
}} | }} | ||
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[[Category: Pal, B.]] | [[Category: Pal, B.]] | ||
[[Category: Sankaranarayanan, R.]] | [[Category: Sankaranarayanan, R.]] | ||
| - | [[Category: SSA]] | ||
[[Category: aminoacyl-trna synthetase]] | [[Category: aminoacyl-trna synthetase]] | ||
[[Category: editing]] | [[Category: editing]] | ||
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[[Category: translation]] | [[Category: translation]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:31:49 2008'' |
Revision as of 00:31, 31 March 2008
| |||||||
| , resolution 2.60Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Activity: | Threonine--tRNA ligase, with EC number 6.1.1.3 | ||||||
| Related: | 1Y2Q, 2HKZ, 2HL0, 2HL1
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of the editing domain of threonyl-tRNA synthetase from Pyrococcus abyssi in complex with an analog of seryladenylate
Overview
To ensure a high fidelity during translation, threonyl-tRNA synthetases (ThrRSs) harbor an editing domain that removes noncognate L-serine attached to tRNAThr. Most archaeal ThrRSs possess a unique editing domain structurally similar to D-aminoacyl-tRNA deacylases (DTDs) found in eubacteria and eukaryotes that specifically removes D-amino acids attached to tRNA. Here, we provide mechanistic insights into the removal of noncognate L-serine from tRNAThr by a DTD-like editing module from Pyrococcus abyssi ThrRS (Pab-NTD). High-resolution crystal structures of Pab-NTD with pre- and post-transfer substrate analogs and with L-serine show mutually nonoverlapping binding sites for the seryl moiety. Although the pre-transfer editing is excluded, the analysis reveals the importance of main chain atoms in proper positioning of the post-transfer substrate for its hydrolysis. A single residue has been shown to play a pivotal role in the inversion of enantioselectivity both in Pab-NTD and DTD. The study identifies an enantioselectivity checkpoint that filters opposite chiral molecules and thus provides a fascinating example of how nature has subtly engineered this domain for the selection of chiral molecules during translation.
About this Structure
2HL2 is a Single protein structure of sequence from Pyrococcus abyssi. Full crystallographic information is available from OCA.
Reference
Post-transfer editing mechanism of a D-aminoacyl-tRNA deacylase-like domain in threonyl-tRNA synthetase from archaea., Hussain T, Kruparani SP, Pal B, Dock-Bregeon AC, Dwivedi S, Shekar MR, Sureshbabu K, Sankaranarayanan R, EMBO J. 2006 Sep 6;25(17):4152-62. Epub 2006 Aug 10. PMID:16902403
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