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[[Image:2hl2.gif|left|200px]]
{{Seed}}
[[Image:2hl2.png|left|200px]]


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{{STRUCTURE_2hl2|  PDB=2hl2  |  SCENE=  }}  
{{STRUCTURE_2hl2|  PDB=2hl2  |  SCENE=  }}  


'''Crystal structure of the editing domain of threonyl-tRNA synthetase from Pyrococcus abyssi in complex with an analog of seryladenylate'''
===Crystal structure of the editing domain of threonyl-tRNA synthetase from Pyrococcus abyssi in complex with an analog of seryladenylate===




==Overview==
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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.
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{{ABSTRACT_PUBMED_16902403}}


==About this Structure==
==About this Structure==
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==Reference==
==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:[http://www.ncbi.nlm.nih.gov/pubmed/16902403 16902403]
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:[http://www.ncbi.nlm.nih.gov/pubmed/16902403 16902403]
A D-amino acid editing module coupled to the translational apparatus in archaea., Dwivedi S, Kruparani SP, Sankaranarayanan R, Nat Struct Mol Biol. 2005 Jun;12(6):556-7. Epub 2005 May 22. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15908961 15908961]
[[Category: Pyrococcus abyssi]]
[[Category: Pyrococcus abyssi]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Enzyme mechanism]]
[[Category: Enzyme mechanism]]
[[Category: Translation]]
[[Category: Translation]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 06:24:57 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 13:11:27 2008''

Revision as of 10:11, 28 July 2008

File:2hl2.png

Template:STRUCTURE 2hl2

Crystal structure of the editing domain of threonyl-tRNA synthetase from Pyrococcus abyssi in complex with an analog of seryladenylate

Template:ABSTRACT PUBMED 16902403

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

A D-amino acid editing module coupled to the translational apparatus in archaea., Dwivedi S, Kruparani SP, Sankaranarayanan R, Nat Struct Mol Biol. 2005 Jun;12(6):556-7. Epub 2005 May 22. PMID:15908961

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