Functional Implications of Domain Organization Within Prokaryotic Rhomboid Proteases.

作者: Rashmi Panigrahi , M. Joanne Lemieux

DOI: 10.1007/978-3-319-23603-2_6

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摘要: Intramembrane proteases are membrane embedded enzymes that cleave transmembrane substrates. This interesting class of enzyme and its water mediated substrate cleavage mechanism occurring within the hydrophobic lipid bilayer has drawn attention researchers. Rhomboids a family ubiquitous serine intramembrane proteases. Bacterial forms rhomboid mainly composed six helices preceded by soluble N-terminal domain. Several crystal structures domain E. coli protease ecGlpG have been solved. Independently, cytoplasmic structure was solved using both NMR protein crystallography. Despite these structures, we still do not know full-length protein, nor functional role domains in cell. chapter will review structural roles different associated with prokaryotic Lastly, address questions remaining field.

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