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Interaction information
Interaction summary
Short label
Glutaminyl-tRNA synthetase-Glutaminyl-tRNA
Full name
Glutaminyl-tRNA synthetase interacts with Glutaminyl-tRNA
Source database
RCSB PDB
ID
1ZJW
Date modified
2011-03-24 18:45:44 JST
Protein information
Short label
Glutaminyl-tRNA synthetase
Full name
Chain A of model 1ZJW: Glutaminyl-tRNA synthetase
Gene
glnS (glutamyl-tRNA synthetase)
GeneID
945310
Official symbol
glnS
Synonyms
2 synonym(s)
Description
glutamyl-tRNA synthetase
Ontologies
2 ontology(s)
Functions
0 function(s)
Processes
1 process(s)
GO:0006418
tRNA aminoacylation for protein translation
Evidence
n/a
Term ID
GO:0006418
Name
tRNA aminoacylation for protein translation
Namespace
biological_process
Definition
The synthesis of aminoacyl tRNA by the formation of an ester bond between the 3'-hydroxyl group of the most 3' adenosine of the tRNA, to be used in ribosome-mediated polypeptide synthesis.
Synonyms
1 synonym(s)
Is-a
1 item(s)
GO:0043039
tRNA aminoacylation
Components
1 component(s)
GO:0005737
cytoplasm
Evidence
n/a
Term ID
GO:0005737
Name
cytoplasm
Namespace
cellular_component
Definition
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
Is-a
1 item(s)
GO:0044424
intracellular part
Origin
Escherichia coli
NCBI Taxonomy ID
562
Name
Escherichia coli
Synonyms
16 synonym(s).
"Bacillus coli" Migula 1895
"Bacterium coli commune" Escherich 1885
"Bacterium coli" (Migula 1895) Lehmann and Neumann 1896
Bacillus coli
Bacterium coli
Bacterium coli commune
Enterococcus coli
Escherchia coli
Escherichia coli (Migula 1895) Castellani and Chalmers 1919
Escherichia coli retron Ec107
Escherichia coli retron Ec67
Escherichia coli retron Ec79
Escherichia coli retron Ec86
Eschericia coli
bacterium 10a
bacterium E3
Cross references
1 item(s)
UniProt
P00962
Sequence
1ZJWA:Glutaminyl-tRNA synthetase
RNA information
Short label
Glutaminyl-tRNA
Full name
Chain B of model 1ZJW: Glutaminyl-tRNA
Sequence
1ZJWB:Glutaminyl-tRNA
Experiments (1)
Experiment 1
gruic-2005
Full name
X-ray diffraction
Detection method
x-ray crystallography (MI:0114)
Term ID
MI:0114
Name
x-ray crystallography
Definition
Analysis of a diffraction pattern generated by a single crystal. X-rays have a wavelength, typically around 1 Angstrom (the diameter of a hydrogen atom). If a narrow parallel beam of X-rays is directed at a sample of a pure protein, most of the X-rays will pass straight through it. A small fraction, however, will be scattered by the atoms in the sample. If the sample is a well-ordered crystal, the scattered waves will reinforce one another at certain points and will appear as diffraction spots when the X-rays are recorded by a suitable detector. The position and intensity of each spot in the X-ray diffraction pattern contain information about the position and nature of the atoms in the crystal. The three-dimensional structure of a large molecule can be deduced from the electron-density map of its crystal. In recent years X-ray diffraction analysis has become increasingly automated, and now the slowest step is likely to be the production of suitable macromolecule crystals. This requires high concentration of very pure macromolecule and empirical searching for the proper crystallisation conditions.
Synonyms
2 synonym(s)
X-ray (PSI-MI-alternate)
x-ray diffraction (PSI-MI-short)
Is-a
2 item(s)
MI:0013
biophysical
MI:0659
experimental feature detection
Host organisms
1 host organism(s)
Origin
Escherichia coli
NCBI Taxonomy ID
562
Name
Escherichia coli
Synonyms
16 synonym(s).
"Bacillus coli" Migula 1895
"Bacterium coli commune" Escherich 1885
"Bacterium coli" (Migula 1895) Lehmann and Neumann 1896
Bacillus coli
Bacterium coli
Bacterium coli commune
Enterococcus coli
Escherchia coli
Escherichia coli (Migula 1895) Castellani and Chalmers 1919
Escherichia coli retron Ec107
Escherichia coli retron Ec67
Escherichia coli retron Ec79
Escherichia coli retron Ec86
Eschericia coli
bacterium 10a
bacterium E3
Reference
GRUIC-SOVULJ, Ita, et al. , J. Biol. Chem. 2005 Jun;280(25):23978-86
PMID
15845536
Title
tRNA-dependent aminoacyl-adenylate hydrolysis by a nonediting class I aminoacyl-tRNA synthetase.
Authors
GRUIC-SOVULJ, Ita, et al.
GRUIC-SOVULJ, Ita
UTER, Nathan
BULLOCK, Timothy
PERONA, John J
Citation
J. Biol. Chem. 2005 Jun;280(25):23978-86
References (1)
Reference 1
GRUIC-SOVULJ, Ita, et al. , J. Biol. Chem. 2005 Jun;280(25):23978-86
PMID
15845536
Title
tRNA-dependent aminoacyl-adenylate hydrolysis by a nonediting class I aminoacyl-tRNA synthetase.
Authors
GRUIC-SOVULJ, Ita, et al.
GRUIC-SOVULJ, Ita
UTER, Nathan
BULLOCK, Timothy
PERONA, John J
Citation
J. Biol. Chem. 2005 Jun;280(25):23978-86
Related articles (1)
Article 1
GRUIC-SOVULJ, Ita, et al. , J. Biol. Chem. 2005 Jun;280(25):23978-86
PMID
15845536
Title
tRNA-dependent aminoacyl-adenylate hydrolysis by a nonediting class I aminoacyl-tRNA synthetase.
Authors
GRUIC-SOVULJ, Ita, et al.
GRUIC-SOVULJ, Ita
UTER, Nathan
BULLOCK, Timothy
PERONA, John J
Citation
J. Biol. Chem. 2005 Jun;280(25):23978-86
Attributes (3)
Attributes
3 attribute(s)
3d-structure
Glutaminyl-tRNA synthetase complexed to glutamine and 2'deoxy A76 glutamine tRNA
3d-resolution
2.500A
3d-r-factors
working 22.000%, free 24.900%