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Structure of the Yersinia type III secretory system chaperone SycE


In the type III secretory system of bacterial pathogens, a large number of sequence-divergent but characteristically small (14–19 kDa), acidic (pl 4–5) chaperone proteins have been identified. We present the 1.74 Å resolution crystal structure of the Yersinia pseudotuberculosis chaperone SycE, whose action in promoting translocation of YopE into host macrophages is essential to Yersinia pathogenesis. SycE, a compact, globular dimer with a novel fold, has two large hydrophobic surface patches that may form binding sites for YopE or other type III components. These patches are formed by structurally key residues that are conserved among many chaperones, suggesting shared structural and functional relationships. A negative electrostatic potential covers almost the entire surface of SycE and is likely conserved in character, but not in detail, among chaperones. The structure provides the first structural insights into possible modes of action of SycE and type III chaperones in general.

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Figure 1: Structure of SycE.
Figure 2: Dimer interface.
Figure 3: Sequence alignment of SycE and related chaperones.
Figure 4: Potential interaction sites.

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We thank J. Bliska for the generous gift of the pYV plasmid, N. Nguyen for excellent technical assistance, G. McDermott for help in MAD data collection, N. Athanasiou for his efforts on this project, M. Marino for help in data analysis and T. Chapman and J. Lawton for critical reading of the manuscript. The Advanced Light Source is supported by the U.S. Department of Energy. S.B. was supported in part by an NIH Molecular Biophysics Training Grant, and P.G. is a recipient of a W.M. Keck Foundation Distinguished Young Scholars in Medicine Award.

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Correspondence to Partho Ghosh.

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Birtalan, S., Ghosh, P. Structure of the Yersinia type III secretory system chaperone SycE. Nat Struct Mol Biol 8, 974–978 (2001).

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