What is it about?
Biotin protein ligase is an enzyme that catalyzes the ATP-dependent biotinylation of a specific lysine residue in acetyl-CoA carboxylase. The biotin±protein ligase from Pyrococcus horikoshii OT3 has been cloned, overexpressed and puri®ed. Crystallization was performed by the microbatch method or the vapour-diffusion method using PEG 2000 as a precipitant at T=295 K. X-ray diffraction data have been collected to 1.6 A resolution from a native crystal and to 1.55 A resolution from a selenomethionine-derivative crystal for multiple anomalous dispersion phasing using synchrotron radiation at 100 K.
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Why is it important?
The native crystal belongs to the monoclinic space group P21, with unit-cell parameters a = 38.601, b = 78.264, c = 70.147 A, = 101.48 . A.
Perspectives
Biotin protein ligase (BPL) mediates the biotinylation of acetyl-CoA carboxylase via the covalent attachment of biotin to a specifc lysine residue of the biotin carboxyl carrier protein (BCCP), which is a core subunit of the carboxylase. We have established the expression, puri®cation and crystallization of PhBPL. The solutions of the liganded forms of the enzyme with biotin, ADP and biotinyl-50-AMP that correspond to distinct func- tional states have been obtained by difference Fourier analyses
Dr Bagautdin Bagautdinov
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This page is a summary of: Crystal structure of the biotin protein ligase fromPyrococcus horikoshiiOT3: insights into the mechanism of biotin activation, Acta Crystallographica Section A Foundations of Crystallography, August 2005, International Union of Crystallography,
DOI: 10.1107/s0108767305091993.
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