Structural highlights
FunctionPublication Abstract from PubMedWe report the 1.9 A 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 beta-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 beta-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 beta-barrel pore in some species and fusion proteins necessary for secreting biofilm-forming exopolysaccharides. The Crystal Structure of Escherichia coli Group 4 Capsule Protein GfcC Reveals a Domain Organization Resembling That of Wza.,Sathiyamoorthy K, Mills E, Franzmann TM, Rosenshine I, Saper MA Biochemistry. 2011 Jun 21;50(24):5465-76. Epub 2011 May 27. PMID:21449614[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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