What is it about?
Biotin-dependent carboxylases play essential roles in the metabolism of all organisms. Their activation by biotinylation is catalysed by biotin protein ligase (BPL). The crystal structures of the archaeal BPL (PhBPL), the biotinyl domain of archaeal biotin carboxyl carrier protein (PhBCCP) and the PhBPL:PhBCCP complex have been determined by X-ray diffraction.
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Why is it important?
The structural feature of the intermediate (biotinyl-5’-AMP) formation was studied using the PhBPL structures liganded with biotin, ATP and biotinyl-5’-AMP [1]. The BPL:BCCP complex was obtained using two BPL mutants R48A and R48A&K111A.
Perspectives
The C-terminal domain of BPL shows large conformational motions to accommodate BCCP, suggesting its functional importance. Additionally, the C-domain has a flexible loop that must open every time when BCCP attaches to BPL, and it allows the specific lysine of BCCP to enter the active site of BPL with the intermediate biotinyl-5’-AMP. These structural details are useful to understand the protein biotinylation which is widely used in purification, quantum dots targeting as well as in the design of anti-obesity drugs.
Dr Bagautdin Bagautdinov
Read the Original
This page is a summary of: X-ray visualization of protein biotinylation, Acta Crystallographica Section A Foundations of Crystallography, August 2008, International Union of Crystallography,
DOI: 10.1107/s0108767308085917.
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