Crystallization and preliminary diffraction studies of TraF, a component of the Escherichia coli type IV secretory system
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‐termin...
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| Veröffentlicht in: | Acta crystallographica. Section D, Biological crystallography. Biological crystallography., 2004-11, Vol.60 (11), p.2025-2027 |
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| container_title | Acta crystallographica. Section D, Biological crystallography. |
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| creator | Audette, Gerald F. Holland, Samantha J. Elton, Trevor C. Manchak, Jan Hayakawa, Koto Frost, Laura S. Hazes, Bart |
| 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 Å, β = 90.40°, and crystals diffract to 2.3 Å resolution. |
| doi_str_mv | 10.1107/S0907444904020724 |
| format | Article |
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Section D, Biological crystallography.</title><addtitle>Acta Cryst. D</addtitle><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 Å, β = 90.40°, and crystals diffract to 2.3 Å resolution.</description><subject>conjugation</subject><subject>Crystallization</subject><subject>Crystallography, X-Ray</subject><subject>Escherichia coli - chemistry</subject><subject>Escherichia coli - metabolism</subject><subject>Escherichia coli Proteins - chemistry</subject><subject>Escherichia coli Proteins - genetics</subject><subject>Escherichia coli Proteins - secretion</subject><subject>F plasmid</subject><subject>Genetic Vectors - genetics</subject><subject>thioredoxin fold</subject><subject>TraF</subject><subject>type IV secretion system</subject><issn>1399-0047</issn><issn>0907-4449</issn><issn>1399-0047</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkM1uEzEUhS1ERUvhAdggr1gx4H-Pl1VIS6UqldoCYmU5nmvFMH-1J4Lh6XFIBEhddGXL93znyh9Cryh5RynR72-JIVoIYYggjGgmnqATyo2pCBH66X_3Y_Q852-EEMa4foaOqZSEcapO0LxIc55c28ZfbopDj13f4DFBG7vYuzTjJoaQnP8zy9O2iZDxEPBdcudvscN-6Mahh37aPU4bwMvsN5Ci38TdsI14mkfAl59xBp9gGkplLhuhe4GOgmszvDycp-jT-fJu8bG6ur64XJxdVZ7Xqq6UbDzXnmrnePCuWXsimZdaCR2UKR-SIkhjWKM8DVoZ4dZM1gBUACeuZvwUvdn3jmm430KebBezh7Z1PQzbbJUyphZGlSDdB30ack4Q7JhiVxxYSuzOt33guzCvD-XbdQfNP-IguATqfeBHbGF-vNGeff2wXEki64JWezQWXT__oi59t0pzLe2X1YUl9erm5pYbq_hvu9ubOw</recordid><startdate>200411</startdate><enddate>200411</enddate><creator>Audette, Gerald F.</creator><creator>Holland, Samantha J.</creator><creator>Elton, Trevor C.</creator><creator>Manchak, Jan</creator><creator>Hayakawa, Koto</creator><creator>Frost, Laura S.</creator><creator>Hazes, Bart</creator><general>Munksgaard International Publishers</general><scope>BSCLL</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>200411</creationdate><title>Crystallization and preliminary diffraction studies of TraF, a component of the Escherichia coli type IV secretory system</title><author>Audette, Gerald F. ; Holland, Samantha J. ; Elton, Trevor C. ; Manchak, Jan ; Hayakawa, Koto ; Frost, Laura S. ; Hazes, Bart</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3868-65dc37c17aa3fcadbc052c57647f6902254f5992d6c1f7694ab258ee14e30a823</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2004</creationdate><topic>conjugation</topic><topic>Crystallization</topic><topic>Crystallography, X-Ray</topic><topic>Escherichia coli - chemistry</topic><topic>Escherichia coli - metabolism</topic><topic>Escherichia coli Proteins - chemistry</topic><topic>Escherichia coli Proteins - genetics</topic><topic>Escherichia coli Proteins - secretion</topic><topic>F plasmid</topic><topic>Genetic Vectors - genetics</topic><topic>thioredoxin fold</topic><topic>TraF</topic><topic>type IV secretion system</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Audette, Gerald F.</creatorcontrib><creatorcontrib>Holland, Samantha J.</creatorcontrib><creatorcontrib>Elton, Trevor C.</creatorcontrib><creatorcontrib>Manchak, Jan</creatorcontrib><creatorcontrib>Hayakawa, Koto</creatorcontrib><creatorcontrib>Frost, Laura S.</creatorcontrib><creatorcontrib>Hazes, Bart</creatorcontrib><collection>Istex</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Acta crystallographica. 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| ispartof | Acta crystallographica. Section D, Biological crystallography., 2004-11, Vol.60 (11), p.2025-2027 |
| issn | 1399-0047 0907-4449 1399-0047 |
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| source | MEDLINE; Wiley Online Library Journals Frontfile Complete; Alma/SFX Local Collection |
| subjects | conjugation Crystallization Crystallography, X-Ray Escherichia coli - chemistry Escherichia coli - metabolism Escherichia coli Proteins - chemistry Escherichia coli Proteins - genetics Escherichia coli Proteins - secretion F plasmid Genetic Vectors - genetics thioredoxin fold TraF type IV secretion system |
| title | Crystallization and preliminary diffraction studies of TraF, a component of the Escherichia coli type IV secretory system |
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