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Structural and Functional Characterization of the VirB5 Protein from the Type IV Secretion System Encoded by the Conjugative Plasmid pKM101

Hye-Jeong Yeo, Qing Yuan, Moriah R. Beck, Christian Baron and Gabriel Waksman
Proceedings of the National Academy of Sciences of the United States of America
Vol. 100, No. 26 (Dec. 23, 2003), pp. 15947-15952
Stable URL: http://www.jstor.org/stable/3149111
Page Count: 6
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Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.
Structural and Functional Characterization of the VirB5 Protein from the Type IV Secretion System Encoded by the Conjugative Plasmid pKM101
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Abstract

Type IV secretion systems mediate intercellular transfer of macromolecules via a mechanism ancestrally related to that of bacterial conjugation machineries. TraC of the IncN plasmid pKM101 belongs to the VirB5 family of proteins, an essential component of most type IV secretion systems. Here, we present the structure of TraC. VirB5/TraC is a single domain protein, which consists of a three helix bundle and a loose globular appendage. Structure-based site-directed mutagenesis followed by functional studies indicates that VirB5 proteins participate in protein-protein interactions important for pilus assembly and function.

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