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6.3.4.15: biotin-[biotin carboxyl-carrier protein] ligase

This is an abbreviated version!
For detailed information about biotin-[biotin carboxyl-carrier protein] ligase, go to the full flat file.

Word Map on EC 6.3.4.15

Reaction

ATP
+
biotin
 +
[biotin carboxyl-carrier protein]-L-lysine
=
AMP
 +
diphosphate
 +
[biotin carboxyl-carrier protein]-N6-biotinyl-L-lysine

Synonyms

Acetyl CoA holocarboxylase synthetase, Acetyl coenzyme A holocarboxylase synthetase, bacterial BirA biotin ligase, biotin acetyl-CoA carboxylase ligase, Biotin holoenzyme synthetase, biotin ligase, biotin protein ligase, Biotin--protein ligase, biotin-protein ligase, Biotin-[acetyl coenzyme A carboxylase] synthetase, Biotin-[acetyl-CoA carboxylase] synthetase, Biotin:apocarboxylase ligase, BirA, BirA protein, BPL, group I biotin protein ligase, HCS, Holocarboxylase synthetase, holocarboxylase synthetase 1, More, STK_15250, Synthetase, biotin-[acetyl coenzyme A carboxylase], yBL

ECTree

     6 Ligases
         6.3 Forming carbon-nitrogen bonds
             6.3.4 Other carbon-nitrogen ligases
                6.3.4.15 biotin-[biotin carboxyl-carrier protein] ligase

Crystallization

Crystallization on EC 6.3.4.15 - biotin-[biotin carboxyl-carrier protein] ligase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant wild-type and mutant R40G enzymes free and in complex with ligands ATP and/or biotin, hanging drop vapour diffusion method, 0.002 ml of protein solution with 5 or 6 mg/ml wild-type or mutant protein, respectively, is mixed with 0.001 ml of reservoir solution containing 0.1M Mes, 0.2 M ammonium sulfate, 15% w/v PEG 5000 monoethyl ether, pH 6.5, with or without 2 mM D-biotin and 5 mM ATP, 17°C, a few hours for the free enzyme, 4-14 days for the complexed enzyme, X-ray diffraction structure determination and analysis at 2.3-2.55 A resolution, molecular modeling
EcBPL domains determination through X-ray crystallography at 2.3 A resolution, and determination of the crystal structure of EcBPL in complex with biotin
purified recombinant enzyme, 0.003 ml of 5 mg/ml protein in 2.5 mM desthiobiotin in 20 mM Tris-HCl pH 8.0, 50 mM NaCl, 1 mM PMSF and 1 mM DTT, is mixed with 0.003 ml of reservoir solution containing 12-16% w/v of both PEG 4000 and PEG 8000 in 0.1 M HEPES, pH 7.5, X-ray diffraction structure determination and analysis at 2.8 A resolution
structures of dehydrated and hydrated BirA, at 2.69 A and 2.8 A resolution, respectively. Dehydration of BirA crystals traps both the apo and active conformations in its asymmetric unit. The crystal lattice rearrangement due to shrinkage in the dehydrated Mtb-BirA crystals ensues structural order of otherwise flexible ligand-binding loops L4 and L8 in apo BirA. In addition, crystal dehydration results in a shift of 3.5 A in the flexible loop L6, a proline-rich loop unique to Mycobacterium tuberculosis complex as well as around the L11 region. The shift in loop L11 in the C-terminal domain on dehydration emulates the action responsible for the complex formation with its protein ligand biotin carboxyl carrier protein domain of ACCA3. The two subunits A and B, though related by a noncrystallographic twofold symmetry, assemble into an asymmetric dimer representing the ligand-bound and ligand-free states of the protein, respectively
structures of the apo-form and in complex with reaction intermediate biotinyl-5'-AMP. Binding of the reaction intermediate leads to clear disorder-to-order transitions. A conserved lysine, Lys138, in the active site is essential for biotinylation
oil-microbatch method using PEG 20000 as a precipitant
-
PhBPL in complex with biotin, ATP and biotinyl-5'-AMP, X-ray diffraction and structure analysis at 1.6 A, 1.6 A, 1.45 A resolution, respectively. Structure-function relationship, modelling, overview
-
purified recombinant enzyme, complexed with biotinyl-5'-AMP, biotin, adenosine, or mutant biotin carboxyl carrier protein PhBCCPN76, X-ray diffraction structure determination at 2.0-2.7 A resolution, analysis, and modelling. The non-hydrolyzable intermediate analogue biotinol-5'-AMP does not provide analyzable complex crystals
-
purified recombinant native and selenomethionine-labeled enzyme comprising residues 1-125, sitting drop method, 9.87 mg/ml protein in 20 mM Tris-HCl, pH 8.0, 500 mM NaCl, 0.001 ml protein solution is mixed with 0.001 ml precipitation solution containing 10.5% PEG 2000, 0.1 M acetate-NaOH, pH 5.5, the drop is overlaid with a 1:1 mixture of silicone and paraffin oil allowing slow water evaporation from the drop, 22°C, preliminary X-ray diffraction structure determination and analysis at 1.45-1.6 A resolution
-
purified recombinant native and selenomethionine-labeled enzyme, sitting drop method, 9.87 mg/ml protein in 20 mM Tris-HCl, pH 8.0, 500 mM NaCl, 0.001 ml protein solution is mixed with 0.001 ml precipitation solution containing 10.5% PEG 2000, 0.1 M acetate-NaOH, pH 5.5, the drop is overlaid with a 1:1 mixture of silicone and paraffin oil allowing slow water evaporation from the drop, 22°C, preliminary X-ray diffraction structure determination and analysis at 1.45-1.6 A resolution
-
apoenzyme, in complex with biotin, and complexed with biotinyl-5'-AMP, hanging drop vapor diffusion method, using
-
hanging drop vapor diffusion method, using 8-12% (w/v) PEG8000 in 0.1 M Tris pH 7.5 or 8.0 and 10% (v/v) glycerol
-
molecular docking of benzoxazolone derivatives in the active site region. Presence of a functional group attached either to the benzene ring or to the pyrole ring incresases binding efficacy
-
purified recombinant enzyme, hanging-drop vapour-diffusion method, 0.001 ml of 15 mg/ml protein solution is mixed with 0.001 ml of reservoir solution containing 8% PEG 8000 and 0.1 M Tris–HCl pH 8.0., at 4°C or 20°C, crystals appear within 24 h, X-ray diffraction structure determination and analysis at 2.3 A resolution
-