Abstract
Peroxins participate in importing necessary proteins into the peroxisomes as well as producing the membrane that separates the peroxisome from the rest of the cell. One of the most powerful ways to elucidate the mechanisms underlying biological phenomena is to determine the three-dimensional structure of the macromolecules and their complexes. This review summarizes recent findings on available structural data of peroxins and their complexes. It provides structure-based mechanistic interpretation of the processes they are involved in, especially, two cases of structural investigations for PTS2 recognition complex that consists of Pex7p, Pex21p and an artificial PTS2-cargo protein, and for the complex of PMP carrier Pex19p and its receptor Pex3p. Recent breakthroughs in cryo-electron microscopy and X-ray free electron lasers have accelerated structural studies of difficult-to-crystallize proteins and have opened up new opportunities in understanding conformational dynamics and visualizing the process of biological actions. Their current results related to peroxins and future prospects are also explained to non-structural biologists.
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Kato, H. (2019). Structure Biology of Peroxisomal Proteins, Peroxins. In: Imanaka, T., Shimozawa, N. (eds) Peroxisomes: Biogenesis, Function, and Role in Human Disease. Springer, Singapore. https://doi.org/10.1007/978-981-15-1169-1_10
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