February 2016

Volume 57Issue 2p157-332
Open Access
COVER: The cover image shows the structure of a cyanobacterial lipoxygenase, which is only distantly related to orthologs from plants and animals. The presented enzyme not only consists of the β-barrel domain (red) and the catalytic domain (grey) containing the nonheme iron (orange sphere), but additionally, an amphipathic helical extension (black) is found at the N-terminus. In contrast to other lipoxygenases, this helical extension rather than the β-barrel domain mediates binding to artificial membranes. Within the catalytic domain, a putative substrate binding channel (blue) was identified, which is defined by amino acids that may position the fatty acid substrate correctly for catalysis. (See Newie et al., p. 276.)...
COVER: The cover image shows the structure of a cyanobacterial lipoxygenase, which is only distantly related to orthologs from plants and animals. The presented enzyme not only consists of the β-barrel domain (red) and the catalytic domain (grey) containing the nonheme iron (orange sphere), but additionally, an amphipathic helical extension (black) is found at the N-terminus. In contrast to other lipoxygenases, this helical extension rather than the β-barrel domain mediates binding to artificial membranes. Within the catalytic domain, a putative substrate binding channel (blue) was identified, which is defined by amino acids that may position the fatty acid substrate correctly for catalysis. (See Newie et al., p. 276.)

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