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Glycyl-tRNA synthetase from Nanoarchaeum equitans: The first crystal structure of archaeal GlyRS and analysis of its tRNA glycylation
- Source :
- Biochemical and biophysical research communications. 511(2)
- Publication Year :
- 2019
-
Abstract
- This study reports the X-ray crystallographic structure of the glycyl-tRNA synthetase (GlyRS) of Nanoarchaeum equitans — a hyperthermophilic archaeal species. This is the first archaeal GlyRS crystal structure elucidated. The GlyRS comprises an N-terminal catalytic domain and a C-terminal anticodon-binding domain with a long β-sheet inserted between these domains. An unmodified transcript of the wild-type N. equitans tRNAGly was successfully glycylated using GlyRS. Substitution of the discriminator base A73 of tRNAGly with any other nucleotide caused a significant decrease in glycylation activity. Mutational analysis of the second base-pair C2G71 of the acceptor stem of tRNAGly elucidated the importance of the base-pair, especially G71, as an identity element for recognition by GlyRS. Glycylation assays using tRNAGly G71 substitution mutants and a GlyRS mutant where Arg223 is mutated to alanine strengthen the possibility that the carbonyl oxygen at position 6 of G71 would hydrogen-bond with the guanidine nitrogen of Arg223 in N. equitans GlyRS.
- Subjects :
- 0301 basic medicine
Glycine-tRNA Ligase
Models, Molecular
Protein Conformation
Archaeal Proteins
Mutant
Biophysics
Aminoacylation
Crystallography, X-Ray
Biochemistry
03 medical and health sciences
chemistry.chemical_compound
0302 clinical medicine
RNA, Transfer
Nanoarchaeum equitans
Nucleotide
Amino Acid Sequence
Guanidine
Molecular Biology
Alanine
chemistry.chemical_classification
DNA ligase
biology
Chemistry
Cell Biology
biology.organism_classification
030104 developmental biology
030220 oncology & carcinogenesis
Transfer RNA
Nanoarchaeota
Sequence Alignment
Subjects
Details
- ISSN :
- 10902104
- Volume :
- 511
- Issue :
- 2
- Database :
- OpenAIRE
- Journal :
- Biochemical and biophysical research communications
- Accession number :
- edsair.doi.dedup.....80699e2c8d90f0a62999800c6a5867ff