Monday, August 5, 2013

Did you know: Scientists have solved the structure of NatA which modifies most human proteins

Protein crystals grown in space:
A collage of protein crystals many of which
were grown on the U.S. Space Shuttle. All the
crystals are useful for X-ray diffraction analysis
NatA, a member of the N-terminal acetyltransferase family of proteins, is an enzyme complex that appears to be essential for the growth of cells. NatA modifies nearly 50% of all other proteins by adding an acetyl group which plays a role in regulating the function of the various proteins. The acetylation of proteins has been shown to regulate protein activity, sub-cellular localization and stability, as well as other protein fuctions. The role of NatA in this process is especially intriguing due to the number of proteins it is capable of modifying and the fact that NatA expression is elevated in cancer cells.

A recent Nature Structural & Molecular Biology paper entitled: 'Molecular basis for N-terminal acetylation by the heterodimeric NatA complex' describes the work which resulted from a colaboration between scientists in the USA and Norway. They employed X-ray crystallography and solved the structure of the entire NatA complex and the structure of the catalytic subunit alone. They found that binding of an auxillary protein induces a conformational change in the catalytic subunit which essentially acts as a switch that turns on the enzymatic activity.

Because of the numerous proteins affected by NatA, and its association with cancer, the authors now seek to identify small molecule inhibitors for NatA. The solved structure will allow them to compare this enzyme to other enzymes with known inhibitors. These inhibitors can then be used as the basis for a directed approach to screen for inhibitory compounds. In order for a compound screen to be performed an enzyme specific assay will need to be designed that can be used in high throughput screening.

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