1n9w
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:1n9w.jpg|left|200px]] | + | [[Image:1n9w.jpg|left|200px]] |
| - | + | ||
| - | '''Crystal structure of the non-discriminating and archaeal-type aspartyl-tRNA synthetase from Thermus thermophilus''' | + | {{Structure |
| + | |PDB= 1n9w |SIZE=350|CAPTION= <scene name='initialview01'>1n9w</scene>, resolution 2.3Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''Crystal structure of the non-discriminating and archaeal-type aspartyl-tRNA synthetase from Thermus thermophilus''' | ||
| + | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1N9W is a [ | + | 1N9W is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N9W OCA]. |
==Reference== | ==Reference== | ||
| - | Non-discriminating and discriminating aspartyl-tRNA synthetases differ in the anticodon-binding domain., Charron C, Roy H, Blaise M, Giege R, Kern D, EMBO J. 2003 Apr 1;22(7):1632-43. PMID:[http:// | + | Non-discriminating and discriminating aspartyl-tRNA synthetases differ in the anticodon-binding domain., Charron C, Roy H, Blaise M, Giege R, Kern D, EMBO J. 2003 Apr 1;22(7):1632-43. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12660169 12660169] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Thermus thermophilus]] | [[Category: Thermus thermophilus]] | ||
| Line 20: | Line 29: | ||
[[Category: biosynthetic protein]] | [[Category: biosynthetic protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:54:03 2008'' |
Revision as of 10:54, 20 March 2008
| |||||||
| , resolution 2.3Å | |||||||
|---|---|---|---|---|---|---|---|
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of the non-discriminating and archaeal-type aspartyl-tRNA synthetase from Thermus thermophilus
Overview
In most organisms, tRNA aminoacylation is ensured by 20 aminoacyl-tRNA synthetases (aaRSs). In eubacteria, however, synthetases can be duplicated as in Thermus thermophilus, which contains two distinct AspRSs. While AspRS-1 is specific, AspRS-2 is non-discriminating and aspartylates tRNA(Asp) and tRNA(Asn). The structure at 2.3 A resolution of AspRS-2, the first of a non-discriminating synthetase, was solved. It differs from that of AspRS-1 but has resemblance to that of discriminating and archaeal AspRS from Pyrococcus kodakaraensis. The protein presents non-conventional features in its OB-fold anticodon-binding domain, namely the absence of a helix inserted between two beta-strands of this fold and a peculiar L1 loop differing from the large loops known to interact with tRNA(Asp) identity determinant C36 in conventional AspRSs. In AspRS-2, this loop is small and structurally homologous to that in AsnRSs, including conservation of a proline. In discriminating Pyrococcus AspRS, the L1 loop, although small, lacks this proline and is not superimposable with that of AspRS-2 or AsnRS. Its particular status is demonstrated by a loop-exchange experiment that renders the Pyrococcus AspRS non-discriminating.
About this Structure
1N9W is a Single protein structure of sequence from Thermus thermophilus. Full crystallographic information is available from OCA.
Reference
Non-discriminating and discriminating aspartyl-tRNA synthetases differ in the anticodon-binding domain., Charron C, Roy H, Blaise M, Giege R, Kern D, EMBO J. 2003 Apr 1;22(7):1632-43. PMID:12660169
Page seeded by OCA on Thu Mar 20 12:54:03 2008
