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.)...Show more
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.)
