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Literature summary for 6.1.1.18 extracted from
- Heat maps for intramolecular communication in an RNP enzyme encoding glutamine (2011), Structure, 19, 386-396.
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| analysis of the crystal structure of GlnRS-tRNAGln complex bound to the glutaminyl adenylate analogue 5'-O-[N-(L-Gln)sulfamoyl] adenosine | Escherichia coli |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| A29X | site-directed mutagenesis | Escherichia coli |
| E323A | site-directed mutagenesis, the mutation produces small but consistent 2 to 3fold improvements in glutamine-binding affinity compared to the wild-type enzyme | Escherichia coli |
| K194A | site-directed mutagenesis, the mutation perturbs the dissociation constant in ATP binding | Escherichia coli |
| K401A | site-directed mutagenesis, the mutant shows reduced kcat compared to the wild-type enzyme | Escherichia coli |
| L136A | site-directed mutagenesis, the mutation perturbs the dissociation constant in ATP binding | Escherichia coli |
| N320A | site-directed mutagenesis, the mutation produces small but consistent 2 to 3fold improvements in glutamine-binding affinity compared to the wild-type enzyme | Escherichia coli |
| N336A | site-directed mutagenesis, the mutation removes contact with the ribose at U38, but does not significantly influence glutamine affinity | Escherichia coli |
| N370A | site-directed mutagenesis, the mutation removes contact with the base of U38, but does not significantly influence glutamine affinity | Escherichia coli |
| Q318A | site-directed mutagenesis, the mutation produces small but consistent 2 to 3fold improvements in glutamine-binding affinity compared to the wild-type enzyme | Escherichia coli |
| Q517A | site-directed mutagenesis, the mutant shows reduced kcat compared to the wild-type enzyme | Escherichia coli |
| R341A | site-directed mutagenesis, the mutation deletes a hydrogen bond made with the O4 moiety of the U35 base | Escherichia coli |
| R341A | site-directed mutagenesis, the mutation removes contact with the base of U35, but does not significantly influence glutamine affinity | Escherichia coli |
| R410A | site-directed mutagenesis, the mutation removes contact with the base of C34, but does not significantly influence glutamine affinity | Escherichia coli |
| R520A | site-directed mutagenesis, the mutant shows reduced kcat compared to the wild-type enzyme | Escherichia coli |
| R545A | site-directed mutagenesis, the mutant shows reduced kcat compared to the wild-type enzyme | Escherichia coli |
| T316A | site-directed mutagenesis, the mutation produces small but consistent 2 to 3fold improvements in glutamine-binding affinity compared to the wild-type enzyme | Escherichia coli |
| T547A | site-directed mutagenesis, the mutant shows reduced kcat compared to the wild-type enzyme | Escherichia coli |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | pre-steady-state kinetics, negative allosteric coupling, overview | Escherichia coli |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | required | Escherichia coli |  |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 64000 | - |
1 * 64000 | Escherichia coli |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | GlnRS forms a 1:1 molar complex with tRNAGln | Escherichia coli | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| monomer | 1 * 64000 | Escherichia coli |
| More | long-range signal propagation from the tRNA anticodon is dynamically driven, whereas shorter pathways are mediated by induced-fit rearrangements, structure modelling, overview | Escherichia coli |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| GlnRS | - |
Escherichia coli |
| Glutaminyl-tRNA synthetase | - |
Escherichia coli |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| ATP | - |
Escherichia coli | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | the architecture of the GlnRS RNP has differentiated over evolutionary time to maintain glutamine-binding affinity at a weak level, and provides strong evidence for long-distance communication | Escherichia coli |
| additional information | generation of a comprehensive mapping of intramolecular communication in the glutaminyl-tRNA synthetase:tRNAGln complex, interaction analysis, detailed overview. Distinct coupling amplitudes for glutamine binding and aminoacyl-tRNA formation on the enzyme, respectively, implying the existence of multiple signaling pathways. Signaling from binding of the tRNA inner elbow, overview. Seven protein contacts with the distal tRNA vertical arm each weaken glutamine binding affinity across distances up to 40 A | Escherichia coli |
| physiological function | negative allosteric coupling plays a key role in enforcing the selective RNA-amino acid pairing at the heart of the genetic code | Escherichia coli |
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