The crystal structure of Escherichia coli group 4 capsule protein GfcC reveals a domain organization resembling that of Wza.

Abstract

We report the 1.9 Å resolution crystal structure of enteropathogenic Escherichia coli GfcC, a periplasmic protein encoded by the gfc operon, which is essential for assembly of group 4 polysaccharide capsule (O-antigen capsule). Presumed gene orthologs of gfcC are present in capsule-encoding regions of at least 29 genera of Gram-negative bacteria. GfcC, a member of the DUF1017 family, is comprised of tandem β-grasp (ubiquitin-like) domains (D2 and D3) and a carboxyl-terminal amphipathic helix, a domain arrangement reminiscent of that of Wza that forms an exit pore for group 1 capsule export. Unlike the membrane-spanning C-terminal helix from Wza, the GfcC C-terminal helix packs against D3. Previously unobserved in a β-grasp domain structure is a 48-residue helical hairpin insert in D2 that binds to D3, constraining its position and sequestering the carboxyl-terminal amphipathic helix. A centrally located and invariant Arg115 not only is essential for proper localization but also forms one of two mostly conserved pockets. Finally, we draw analogies between a GfcC protein fused to an outer membrane β-barrel pore in some species and fusion proteins necessary for secreting biofilm-forming exopolysaccharides.

DOI: 10.1021/bi101869h

Cite this paper

@article{Sathiyamoorthy2011TheCS, title={The crystal structure of Escherichia coli group 4 capsule protein GfcC reveals a domain organization resembling that of Wza.}, author={Karthik Sathiyamoorthy and Erez Mills and Titus M. Franzmann and Ilan Rosenshine and Mark A Saper}, journal={Biochemistry}, year={2011}, volume={50 24}, pages={5465-76} }