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Permanent link (DOI): https://doi.org/10.7939/R3HH6CH1Q

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Crystallization and preliminary diffraction studies of TraF, a component of the Escherichia coli type IV secretory system Open Access

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Author or creator
Audette, G.F.
Holland, S.J.
Manchak, J.
Hayakawa, K.
Frost, L.S.
Hazes, B.
Additional contributors
Subject/Keyword
bacteria
proteins
plasmids
conjugation
Type of item
Journal Article (Published)
Language
English
Place
Time
Description
TraF, a component of the Escherichia coli type IV secretory system, has been crystallized and preliminary X-ray diffraction data have been collected. TraF is a 26 kDa protein encoded by the E. coli F plasmid and is required for conjugative plasmid transfer and the formation of sex pili. The N-terminal domain of TraF has no recognizable sequence features, whereas the C-terminal domain is believed to adopt a thioredoxin fold. However, since the active-site cysteines of thioredoxin-like proteins are not conserved in TraF, its biochemical role remains unclear. TraF crystallizes in space group C2, with unit-cell parameters a = 119.87, b = 34.36, c = 46.21 A, β= 90.40°, and crystals diffract to 2.3 A resolution.
Date created
2004
DOI
doi:10.7939/R3HH6CH1Q
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© 2004 International Union of Crystallography
Citation for previous publication
GF Audette, SJ Holland, J Manchak, K Hayakawa, LS Frost and B Hazes. "Crystallization and preliminary diffraction studies of TraF, a component of the Escherichia coli type IV secretory system." Acta Crystallographica Section D Biological Crystallography 60 (2004): 2025-2027.
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