EsxB, a secreted protein from B acillus anthracis forms two distinct helical bundles: Structure of Secreted EsxB and its Variants
- Midwest Center for Structural Genomics, Argonne National Laboratory, Argonne Illinois 60439
- Midwest Center for Structural Genomics, Argonne National Laboratory, Argonne Illinois 60439; Department of Biosciences, Structural Biology Center, Argonne National Laboratory, Argonne Illinois 60439; Center for Structural Genomics of Infectious Diseases, University of Chicago, Chicago Illinois 60637
- Howard Taylor Ricketts Laboratory, Argonne National Laboratory, Argonne Illinois 60439; Department of Microbiology, University of Chicago, Chicago Illinois 60637
The EsxB protein from Bacillus anthracis belongs to the WXG100 family, a group of proteins secreted by a specialized secretion system. We have determined the crystal structures of recombinant EsxB and discovered that the small protein (~10 kDa), comprised of a helix-loop-helix (HLH) hairpin, is capable of associating into two different helical bundles. The two basic quaternary assemblies of EsxB are an antiparallel (AP) dimer and a rarely observed bisecting U (BU) dimer. This structural duality of EsxB is believed to originate from the heptad repeat sequence diversity of the first helix of its HLH hairpin, which allows for two alternative helix packing. The flexibility of EsxB and the ability to form alternative helical bundles underscore the possibility that this protein can serve as an adaptor in secretion and can form hetero-oligomeric helix bundle(s) with other secreted members of the WXG100 family, such as EsxW. The highly conserved WXG motif is located within the loop of the HLH hairpin and is mostly buried within the helix bundle suggesting that its role is mainly structural. The exact functions of the motif, including a proposed role as a secretion signal, remain unknown.
- Research Organization:
- Argonne National Laboratory (ANL), Argonne, IL (United States)
- Sponsoring Organization:
- National Institutes of Health (NIH); USDOE Office of Science - Office of Biological and Environmental Research
- DOE Contract Number:
- AC02-06CH11357
- OSTI ID:
- 1391889
- Journal Information:
- Protein Science, Vol. 24, Issue 9; ISSN 0961-8368
- Publisher:
- The Protein Society
- Country of Publication:
- United States
- Language:
- English
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