6.3.4.19: tRNAIle-lysidine synthase

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For detailed information about tRNAIle-lysidine synthase, go to the full flat file.

Reaction

Synonyms

lysidine synthetase, mesJ, MesJ protein, TilS, TilS protein, tRNAIle lysidine synthetase, tRNAIle-lysidine synthetase, yacA

ECTree

     6 Ligases

         6.3 Forming carbon-nitrogen bonds

             6.3.4 Other carbon-nitrogen ligases

                6.3.4.19 tRNAIle-lysidine synthase

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Results	in table
43164	AA Sequence
3	Application
1	CAS Registry Number
7	Cloned(Commentary)
4	Crystallization (Commentary)
10	General Information
23	IC50 Value
23	Inhibitors
2	kcat/KM [mM/s]
33	KM Value [mM]
11	Natural Substrates/ Products (Substrates)
116	Organism
1	pH Optimum
14	Protein Variants
5	Purification (Commentary)
1	Reaction
16	Reference
27	Substrates and Products (Substrate)
2	Subunits
25	Synonyms
1	Systematic Name
7	Turnover Number [1/s]

Crystallization

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Crystallization on EC 6.3.4.19 - tRNAIle-lysidine synthase

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

crystal structure of Aquifex aeolicus TilS, complexed with ATP, Mg2+, and L-lysine, at 2.5 A resolution. The presence of the TilS-specific subdomain causes the active site to have two separate gateways, a large hole and a narrow tunnel on the opposite side. ATP is bound inside the hole, and L-lysine is bound at the entrance of the tunnel. The conserved Asp36 in the PP-motif coordinates Mg2+. In these initial binding modes, the ATP, Mg2+, and L-lysine are held far apart from each other, but they seem to be brought together for the reaction upon cytidine binding, with putative structural changes of the complex

Aquifex aeolicus

O67728

706782

crystal structure of TilS at 2.42 A resolution. Structural and functional comparisons with Escherichia coli TilS reveals that the two TilS enzymes discriminate premodified tRNAIle2 from premodified tRNAMet by strategies similar to that used by IleRS, but in distinct manners

Aquifex aeolicus

O67728

706481

structural and functional comparisons of Escherichia coli TilS and Axifex aeolicus TilS reveal that the two TilS enzymes discriminate premodified tRNAIle2 from premodified tRNAMet bystrategies similar to that used by IleRS, but in distinct manners

Escherichia coli

-

706481

crystal structure of Geobacillus kaustophilus TilS complexed with Bacillus subtilis tRNAIle CAU at 3.65 A resolution, by the multiwavelength anomalous dispersion method. The asymmetric unit contains one TilS homodimer and two tRNAs, each tightly embedded in one monomer of TilS, with an overall interface of 2998 A. Each monomer consists of an amino-terminal catalytic domain, and two carboxy-terminal domains, connected by a long a-helical linker and a loop linker, respectively

Geobacillus kaustophilus

Q5L3T3

705888