2hz7
From Proteopedia
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'''Crystal structure of the Glutaminyl-tRNA synthetase from Deinococcus radiodurans''' | '''Crystal structure of the Glutaminyl-tRNA synthetase from Deinococcus radiodurans''' | ||
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[[Category: Paulus, C.]] | [[Category: Paulus, C.]] | ||
[[Category: Sauter, C.]] | [[Category: Sauter, C.]] | ||
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| - | [[Category: | + | [[Category: Glnrs core]] |
| - | [[Category: | + | [[Category: Rossmann fold]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 06:53:24 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 03:53, 4 May 2008
Crystal structure of the Glutaminyl-tRNA synthetase from Deinococcus radiodurans
Overview
Glutaminyl-tRNA synthetase from Deinococcus radiodurans possesses a C-terminal extension of 215 residues appending the anticodon-binding domain. This domain constitutes a paralog of the Yqey protein present in various organisms and part of it is present in the C-terminal end of the GatB subunit of GatCAB, a partner of the indirect pathway of Gln-tRNA(Gln) formation. To analyze the peculiarities of the structure-function relationship of this GlnRS related to the Yqey domain, a structure of the protein was solved from crystals diffracting at 2.3 A and a docking model of the synthetase complexed to tRNA(Gln) constructed. The comparison of the modeled complex with the structure of the E. coli complex reveals that all residues of E. coli GlnRS contacting tRNA(Gln) are conserved in D. radiodurans GlnRS, leaving the functional role of the Yqey domain puzzling. Kinetic investigations and tRNA-binding experiments of full length and Yqey-truncated GlnRSs reveal that the Yqey domain is involved in tRNA(Gln) recognition. They demonstrate that Yqey plays the role of an affinity-enhancer of GlnRS for tRNA(Gln) acting only in cis. However, the presence of Yqey in free state in organisms lacking GlnRS, suggests that this domain may exert additional cellular functions.
About this Structure
2HZ7 is a Single protein structure of sequence from Deinococcus radiodurans. Full crystallographic information is available from OCA.
Reference
Deinococcus glutaminyl-tRNA synthetase is a chimer between proteins from an ancient and the modern pathways of aminoacyl-tRNA formation., Deniziak M, Sauter C, Becker HD, Paulus CA, Giege R, Kern D, Nucleic Acids Res. 2007;35(5):1421-31. Epub 2007 Feb 6. PMID:17284460 Page seeded by OCA on Sun May 4 06:53:24 2008
