Any feedback?
Please rate this page
(all_enzymes.php)
(0/150)

BRENDA support

6.1.1.4: leucine-tRNA ligase

This is an abbreviated version!
For detailed information about leucine-tRNA ligase, go to the full flat file.

Word Map on EC 6.1.1.4

Reaction

ATP
+
L-leucine
 +
tRNALeu
=
AMP
 +
diphosphate
 +
L-leucyl-tRNALeu

Synonyms

AaLeuRS, alphabeta-LeuRS, b0642, cytoplasmic LeuRS, EcLeuRS, GlLeuRS, HcleuRS, hs mt LeuRS, JW0637, LARS, LARS1, LARS2, Leucine translase, Leucine--tRNA ligase, Leucyl-transfer ribonucleate synthetase, Leucyl-transfer ribonucleic acid synthetase, Leucyl-transfer RNA synthetase, leucyl-tRNA ligase, leucyl-tRNA syntethase, Leucyl-tRNA synthetase, leucyl-tRNA synthetase 1, leucyl—tRNA synthetase, LeuRS, LeuRS1, LeuRS2, LeuRSTT, leuS, LRS, MmLeuRS, More, mt leucyl-tRNA synthetase, mt-LeuRS, mtLeuRS, PhLeuRS, Synthetase, leucyl-transfer ribonucleate, ycLeuRS

ECTree

     6 Ligases
         6.1 Forming carbon-oxygen bonds
             6.1.1 Ligases forming aminoacyl-tRNA and related compounds
                6.1.1.4 leucine-tRNA ligase

Crystallization

Crystallization on EC 6.1.1.4 - leucine-tRNA ligase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
structure at 2.2 A resolution of the editing domain in complex with compound AN3018, i.e.6-(ethylamino)-5-fluorobenzo[c][1,2]oxaborol-1(3H)-ol, using AMP as a surrogate for the 3' adenosine of tRNAleu. Comparison with the structure of the human enzyme
-
crystal and cocrystal structures for LeuRS, IleRS, and ValRS suggests that the CP1 domain rotates via its flexible beta-strand linkers relative to the main body along various steps in the enzymeÂ’s reaction pathway. Computational analysis suggested that the end of the N-terminal beta-strand acted as a hinge. A molecular hinge might specifically direct movement of the CP1 domain relative to the main body
-
crystal structure of editing domain of Escherichia coli LeuRS in both apo form and complexes with methionine and isoleucine at 2.0 A, 2.4 A, and 3.2 A resolution, hanging drop vapour diffusion method
enzyme LeuRS mutant T252A in a complex with tRNALeu and leucyl-adenylate sulphamoyl analogue (Leu-AMS), both positioned in the synthetic active site, and Leu2AA located in the editing domain, X-ray diffraction structure determination and analysis at resolution, replacement using structure PDB ID 4AQ7, modeling
structure of the selenomethionine-labeled CP1 domain to 3.25 A, comparison with the structure of Candida albicans enzyme
-
hanging drop vapor diffusion method, using 0.1 M bis-Tris (pH 5.5), 0.6 M ammonium acetate, and 20% (w/v) PEG3350 at 4°C
Mesomycoplasma mobile
-
cocrystallizations with each of the tRNALeu isoacceptors are attempted. Cocrystals are obtained by the hanging-drop vapour-diffusion method, but only when the tRNALeu isoacceptor with the anticodon CAA is used. Electrophoretic analyses reveals that the crystals contain both leucyl-tRNA synthetase and tRNALeu, suggesting that they are LeuRS-tRNALeu complex crystals. A data set diffracting to 3.3 A resolution is collected from a single crystal at 100 K. The crystal belongs to the orthorhombic space group P2(1)2(1)2, with unit-cell parameters a = 118.18, b = 120.55, c = 231.13 A
-
hanging-drop vapour-diffusion method using ammonium sulfate as a precipitant. The crystals belong to the rhombohedral space group R3, with unit-cell parameters a = b = 186.20, c = 91.43 A, alpha = beta = 90, gamma = 120°. The asymmetric unit contains one molecule of LeuRS, with a corresponding crystal volume per protein weight of 3.2 A3 Da(-1) and a solvent content of 60.7%. A data set diffracting to 2.2 A resolution is collected from a single crystal at -173°C. Selenomethionine-substituted protein crystals are prepared in order to solve the structure by the SAD phasing method
-
hanging-drop vapour-diffusion method, resolution 2.1 A, C-terminally truncated LeuRS (amino acids 1-810), crystals belong to the Rhombohedral space group R3, with unit-cell parameters a = b = 186.23 A, c = 91.45 A, alpha = beta = 90°, gamma = 120° for the native form and a = b = 185.8 A, c = 91.19 A, alpha = beta = 90°, and gamma = 120° for the SeMet crystal
-
construction of a structural model of the completely solvated leucyl-tRNA synthetase complexed with valyl-tRNALeu
crystal growth in presence of mercuric chloride, soaking of the crystals in solution containing 0.6 mM of the non-hydrolyzable substrate analogue norvaline-AMS for 1 month, or cocrystallization of enzyme and norvaline-AMS, X-ray diffraction structure determinationat 2.0-2.2 A resolution and analysis
crystal structure of leucyl-tRNA synthetase complexed with tRNALeu in the post-transfer-editing conformation, crystals of the complex are grown at 20°C by hanging drop vapour diffusion
-
crystallization of enzyme alone or in complex with leucine or leucyl-adenylate analogue, and crystallization of selenomethionine-enzyme, hanging-drop vapour-diffusion method with ammonium sulfate as precipitant, X-ray diffraction structure determination at 1.9-6 A resolution
-