What is it about?
We have determined the three-dimensional (3D) structure of a protein complex related to the metabolic syndrome. Organisms have an energy storage system in which excess calories are converted into adipose (fatty acid) for emergencies. However, in human beings, this system could be the main reason for metabolic syndrome disorders including cardiac disorder and cerebral stroke. These diet-induced diseases and obesity can be overcome by regulating the activity of acetyl-CoA carboxylase (ACC), which is a key enzyme in fatty acid biosynthesis. It is reported that ACC-deficient mutant mice have a normal life span, a high fatty acid oxidation rate, and low amounts of fat.
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Why is it important?
It is apparent that the recognition of the biotinyl domain is a rather complex process. This is in contrast with most other post-translational modifications in which the primary structure surrounding the target residue can be of crucial importance. BPL and BCCP have several mobile parts that are essential for the biotinylation reaction in multiple stages: BCCP binding (formation stages 1 and 2), catalysis (reaction stage), and product release (product stage).
Perspectives
Learning how the biotinylation factors are choreographed to accomplish protein biotinylation with extreme substrate specificity remains an unmet challenge for investigators.
Dr Bagautdin Bagautdinov
Read the Original
This page is a summary of: Protein Biotinylation Visualized by a Complex Structure of Biotin Protein Ligase with a Substrate, Journal of Biological Chemistry, May 2008, Elsevier,
DOI: 10.1074/jbc.m709116200.
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