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  Protein circlets as sex pilus subunits

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

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 Creators:
Kalkum, Markus1, Author
Eisenbrandt, Ralf1, Author
Lanka, Erich1, Author
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1Max Planck Society, ou_persistent13              

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 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.

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Language(s): eng - English
 Dates: 2004
 Publication Status: Issued
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 Rev. Type: -
 Identifiers: eDoc: 230579
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Title: Current Protein & Peptide Science
Source Genre: Journal
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Pages: - Volume / Issue: 5 (5) Sequence Number: - Start / End Page: 417 - 424 Identifier: ISSN: 1389-2037