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Caption
The structure of NatA, an n-terminal acetyltransferase, is described in a paper published Aug. 4, 2013, in Nature Structural & Molecular Biology.
Credit
The Wistar Institute/Glen Liszczak
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In the August 4, 2013 issue of Nature & Structural Molecular Biology researchers from The Wistar Institute, the University of Pennsylvania, and the University of Bergen published the structure of an enzyme
called NatA, which has a role in modifying proteins and is found in increased amounts in cancer cells.
Their findings, they believe, will help in creating an inhibitor against NatA that may curb the spread of cancerous cells.
What follows is a brief animation of the enzyme's structure and the shape changes that occur to the enzyme when another molecule
binds to it.
An overall view of the NatA complex structure.
The complex is shown rotating 360° on the y-axis
followed by 360° on the x-axis.
The NatA active site (Naa10p) changes
shape upon binding to a site called Naa15p. This movie shows a morph that highlights
the change in the position of several key residues. The morph is shown twice, once
with acetyl CoA bound to Naa10p and again with an inhibitor bound to Naa10p.