Protein Structure
Like eukaryotic intermediate filaments, crescentin organizes into filaments and is present in a helical structure in the cell. Crescentin is necessary for both shapes of the Caulobacter prokaryote (vibroid/crescent-shape and helical shape, which it may adopt after a long stationary phase). The crescentin protein has 430 residues; its sequence mostly consists of a pattern of 7 repeated residues which form a coiled-coil structure. The DNA sequence of the protein has sections very similar to the eukaryotic keratin and lamin proteins, mostly involving the coiled-coil structure. Researchers Ausmees et al. recently proved that, like animal intermediate filament proteins, crescentin has a central rod made up of four coiled-coil segments. Both intermediate filament and crescentin proteins have a primary sequence including four α-helical segments along with non-α-helical linker domains. An important difference between crescentin and animal intermediate filament proteins is that crescentin lacks certain consensus sequence elements at the ends of the rod domain which are conserved in animal lamin and keratin proteins.
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