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The structure of the extraordinarily stable dimeric B domain of streptococcal protein G has been determined at 1.65 A resolution. This recombinant protein, which lacks the natural C-terminal domain and contains additional stabilizing mutations, has a T(m) of 89 degrees C and survives denaturation in 8 M urea and 25 degrees C for 12 h. The N-terminal half of the structure is a tandem repeat of three alpha/beta motifs, but the overall fold is very different from those of beta-sheet proteins. Most surprising is the peculiar conformation of a putative helix in the middle of the structure, a parallel beta-strand that occupies a distinct position. This unprecedented, disordered strand prevents the association of its C-terminal region to the C-terminal parts of the domain, which are completely ordered. This interaction is driven by hydrophobic contacts and a hydrogen bond.The Australian Greens today announced a $1.5 million campaign against the legislation to prevent us from making our own decisions about our health and reproduction.
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