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The type II secretion arrowhead: the structure of GspI–GspJ–GspK

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A heterotrimeric complex of minor pseudopilins from the type II secretion system has been identified and its crystal structure solved. Although each subunit shares the same overall α-β fold as other characterized (pseudo)pilins, GspK has a unique large α-helical domain inserted between two canonical β-strands. The structure constrains models for pseudopilus assembly.

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Figure 1: Hypothetical models for secretion piston action versus pseudopilus assembly.

Katie Ris-Vicari

Figure 2: Structural similarity between the GspK α-domain and the Thermus thermophilus ComEA homolog (PDFB 2DUY) GspK residues 93–198 (cartoon; reverse-rainbow shading from blue N terminus to red C terminus) and residues 16–75 of the ComEA homolog (gray snake, PDB 2DUY) adopt the same fold, with a 1.4-Å r.m.s. deviation over 100 most well-matched atoms or a 1.9-Å r.m.s. deviation over 59 Cα atoms.

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  1. Katrina T. Forest is at the Department of Bacteriology, University of Wisconsin-Madison, 1550 Linden Drive, Madison, Wisconsin 53706, USA. forest@bact.wisc.edu,

    Katrina T Forest

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  1. Katrina T Forest
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Forest, K. The type II secretion arrowhead: the structure of GspI–GspJ–GspK. Nat Struct Mol Biol 15, 428–430 (2008). https://doi.org/10.1038/nsmb0508-428

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