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Journal Article

Protein circlets as sex pilus subunits

MPS-Authors

Kalkum,  Markus
Max Planck Society;

Eisenbrandt,  Ralf
Max Planck Society;

Lanka,  Erich
Max Planck Society;

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Kalkum, M., Eisenbrandt, R., & Lanka, E. (2004). Protein circlets as sex pilus subunits. Current Protein & Peptide Science, 5(5), 417-424.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0010-8932-8
Abstract
The largest circular protein structures discovered define a class of transfer proteins acting in bacterial conjugation and type IV secretion. Proteins ranging from 73 to 78 residues with head-to-tail peptide bonds constitute the major subunit of conjugative pili of some type IV secretion systems. Their plasmid-encoded precursors are enzymatically processed and cyclized before being assembled into pili. These extra-cellular surface filaments mediate physical contact between donor and recipient cell or pathogen and host cell. Pili are essential prerequisites for DNA and protein transfer. A membrane-bound signal peptidase-like enzyme is responsible for the circularization reaction. Site-directed mutagenesis and mass spectrometry has been used extensively to unravel the mechanism of the enzyme-substrate interaction of the pilin maturation process.