What is it about?
Biotin protein ligase catalyses the biotinylation of the biotin carboxyl carrier protein subunit of acetyl-CoA carboxylase. To elucidate the exact details of the protein–protein interactions in the biotinylation function, the C-terminal half fragment of BCCP, the R48A mutant of BPL and the R48A K111A double mutant of BPL were crystallized.
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Why is it important?
We considered the structural details of the second step of the biotinylation reaction in which the activated biotin is transferred to a specific lysine of the BCCP subunit of acetyl-CoA carboxylase have not yet been resolved.
Perspectives
We have for the first time captured the BPL complex states containing biotin and partly disordered ATP. These structures will be a good foothold to obtain valuable information regarding molecular recognition and interaction in the BPL–BCCP system.
Dr Bagautdin Bagautdinov
Read the Original
This page is a summary of: Crystallization and preliminary X-ray crystallographic studies of the biotin carboxyl carrier protein and biotin protein ligase complex fromPyrococcus horikoshiiOT3, Acta Crystallographica Section F Structural Biology and Crystallization Communications, March 2007, International Union of Crystallography,
DOI: 10.1107/s1744309107011967.
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