Protein circlets as sex pilus subunits

Kalkum, Markus; Eisenbrandt, Ralf; Lanka, Erich

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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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Item Permalink: https://hdl.handle.net/11858/00-001M-0000-0010-8932-8 Version Permalink: https://hdl.handle.net/11858/00-001M-0000-0010-8933-6

Genre: Journal Article

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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: Date issued: 2004

Publication Status: Issued

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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