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6.2.1.33: 4-chlorobenzoate-CoA ligase

This is an abbreviated version!
For detailed information about 4-chlorobenzoate-CoA ligase, go to the full flat file.

Word Map on EC 6.2.1.33

Reaction

4-Chlorobenzoate
+
CoA
 +
ATP
=
4-chlorobenzoyl-CoA
 +
AMP
 +
diphosphate

Synonyms

4-CB:CoA ligase, 4-CBA:CoA ligase, 4-chlorobenzoate:CoA ligase, 4-Chlorobenzoate:coenzyme A ligase, 4-Chlorobenzoyl-CoA ligase, 4-Chlorobenzoyl-coenzyme A ligase, 4-Halobenzoate-coenzyme A ligase, CBAL, CBL, chlorobenzoate:CoA ligase, Synthetase, 4-chlorobenzoyl coenzyme A

ECTree

     6 Ligases
         6.2 Forming carbon-sulfur bonds
             6.2.1 Acid-thiol ligases
                6.2.1.33 4-chlorobenzoate-CoA ligase

Crystallization

Crystallization on EC 6.2.1.33 - 4-chlorobenzoate-CoA ligase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, 1.0 and 2.2 A. Crystal structures of the enzyme both in the unliganded state and bound to 4-chlorobenzoate. The space group is P3(1)21 or P3(2)21 with a = b = 129.3 A, c = 71.5 A
-
purified recombinant CBL bound to 4-chlorobenzoyl-AMP, hanging drop vapor diffusion at 4°C using 16-24% pentaerythritol propoxylate 426, and 0.1 M K+-HEPES, pH 6.5 or 6.75, and optimized via hanging drop vapor diffusion using 14-18% PEG 1000, 50-100 mM magnesium nitrate and 100 mM MOPS, pH 7.0, the cryoprotectant contains 24% pentaerythritol propoxylate 426, 24% ethylene glycol, and 0.1 M K+-HEPES, 1 mM ATP, and 1 mM 4-chlorobenzoate, X-ray diffraction structure determination and analysis at 2.0-2.25 A resolution, molecular replacement
purified recombinant enzyme, X-ray diffraction structure determination and analysis, modelling
mutant D402P, to 2.6 A resolution, and comparison with wild-type. The C-terminal domain rotates by about 140 degrees between the two states that catalyze the adenylation and thioester-forming half-reactions. The domain rotation is accompanied by a change in the main chain torsional angles of residue D402