6.1.1.10: methionine-tRNA ligase
This is an abbreviated version!
For detailed information about methionine-tRNA ligase, go to the full flat file.
Word Map on EC 6.1.1.10
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6.1.1.10
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synthetases
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aminoacyl-trna
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aminoacylation
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anticodons
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homocysteine
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trnafmet
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thiolactone
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aarss
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isoleucyl-trna
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trypsin-modified
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isoleucylation
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noncognate
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tyrosyl-trna
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arc1p
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atp-ppi
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formylmethionine
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medicine
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leucyl-trna
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kmsks
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misacylation
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hcy-thiolactone
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ilers
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lysyl-trna
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trna-binding
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valrs
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valyl-trna
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cysteinyl-trna
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drug development
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pharmacology
- 6.1.1.10
- synthetases
- aminoacyl-trna
- aminoacylation
-
anticodons
- homocysteine
- trnafmet
-
thiolactone
-
aarss
-
isoleucyl-trna
-
trypsin-modified
-
isoleucylation
-
noncognate
- tyrosyl-trna
- arc1p
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atp-ppi
- formylmethionine
- medicine
- leucyl-trna
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kmsks
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misacylation
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hcy-thiolactone
- ilers
- lysyl-trna
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trna-binding
- valrs
- valyl-trna
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cysteinyl-trna
- drug development
- pharmacology
Reaction
Synonyms
hcMetRS, hmMetRS, let-65, MARS, mars-1, MetG, Methionine translase, Methionine--tRNA ligase, Methionyl tRNA synthetase, Methionyl-transfer ribonucleate synthetase, Methionyl-transfer ribonucleic acid synthetase, Methionyl-transfer RNA synthetase, methionyl-tRNA synthetase, methionyl-tRNA synthetase1, methionyl-tRNA-synthetase, MetRS, MetRS1, MetRS2, MetS, More, MRS, MRSapi, MRScyt, Synthetase, methionyl-transfer ribonucleate
ECTree
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Subunits
Subunits on EC 6.1.1.10 - methionine-tRNA ligase
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dimer
homodimer
monomer
tetramer
additional information
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x * 84000, recombinant protein 1 expressed in Escherichia coli, SDS-PAGE
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2 * 85000, SDS-PAGE after boiling the enzyme in 2% SDS and 1% mercaptoethanol, reduction and carboxymethylation in 6 M guanidine hydrochloride
dimer
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2 * 85000, SDS-PAGE after boiling the enzyme in 2% SDS and 1% mercaptoethanol, reduction and carboxymethylation in 6 M guanidine hydrochloride
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dimer
2 * 12000, recombinant protein 2 expressed in Escherichia coli, SDS-PAGE
monomer
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mutant D666A ia monomeric, M665 mutant is monomeic in absence of NgCl2, and dimeric in presence of 10 mM MgCl2, native PAGE
monomer
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1 * 62000, recombinant truncated mutant enzyme, mass spectrometry
monomer
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MetRs is a monomeric multidomain enzyme, comparisons with other MetRS structures. The MetRS core unit consists of four domains: the catalytic domain, the CP domain, the KMSKS domain, and an anticodon-binding domain.the enzyme crystal structure contains a KMSKS(301-305) loop in proximity to the catalytic site in an open and inactive conformation, overview
monomer
1 * 66500, truncated enzyme, SDS-PAGE, 1 * 89700, wild-type enzyme, SDS-PAGE
monomer
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1 * 78000, SDS-PAGE, fully active monomeric enzyme derived from high-molecular-weight complexes by controlled proteolysis
additional information
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MetRS is a multidomain protein, structural organization: the very C-terminal appended domain is related to the oligonucleotide binding-fold-based tRNA-binding domain recovered at the C-terminus of MetRS from plant, but, in the nematode enzyme, this domain is separated from the core enzyme by an insertion domain
additional information
secondary structure and three-dimensional structure molecular modeling, model validation, overview
additional information
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secondary structure and three-dimensional structure molecular modeling, model validation, overview
additional information
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secondary structure and three-dimensional structure molecular modeling, model validation, overview
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additional information
domain structure, structure modeling based on crystal structures of Escherichia coli with PDB code 1QQR, overview, the enzyme contains the consensus motifs of class I aminoacyl-tRNA, but lacks the Zn2+ binding motif and the C-terminal dimerization region
additional information
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domain structure, structure modeling based on crystal structures of Escherichia coli with PDB code 1QQR, overview, the enzyme contains the consensus motifs of class I aminoacyl-tRNA, but lacks the Zn2+ binding motif and the C-terminal dimerization region
additional information
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structure of LmMetRS in complex with two products, methionyladenylate and diphosphate, along with a Mg2+ ion that bridges them, the residues of the class I aaRS signature sequence motifs, KISKS and HIGH, make numerous contacts with the diphosphate, structure comparisons, overview
additional information
at high protein concentration the enzyme can form a dimer in vitro
additional information
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at high protein concentration the enzyme can form a dimer in vitro
additional information
dimerization of the enzyme is required for affinity to tRNAMet
additional information
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dimerization of the enzyme is required for affinity to tRNAMet
additional information
three-dimensional structure, structure of the dimerization domain
additional information
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three-dimensional structure, structure of the dimerization domain
additional information
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three-dimensional structure of MetRS by homology modeling method, overview
additional information
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homology modeling and ligand docking studies of trypanosomatid MetRS enzymes, structure comparisons, overview