Researchers used cryo-electron microscopy to capture the first atomic-level view of N-myristoyltransferase 2 (NMT2) working on a ribosome alongside the nascent polypeptide-associated complex (NAC). They found NAC actively recruits NMT2 to translating ribosomes, doubling its binding efficiency. Together, NMT2 and NAC form a continuous channel that guides newly made proteins directly from the ribosomal exit tunnel into NMT2's catalytic site, where a fatty acid tag (myristoyl group) is added. A ribosomal RNA clamp further stabilizes the complex. This process is essential for correct protein localization to cell membranes and is dysregulated in cancers and heart disease, making NMT2 a compelling therapeutic target.
