Thank you for visiting nature.com. You are using a browser version with limited support for CSS. To obtain
the best experience, we recommend you use a more up to date browser (or turn off compatibility mode in
Internet Explorer). In the meantime, to ensure continued support, we are displaying the site without styles
and JavaScript.
Hydroxylamine oxidoreductase performs the second step in the oxidation of ammonium to nitrite, a critical part of the nitrogen cycle. Its structure reveals a complex arrangement of haems that could serve to direct electrons along two separate pathways.
The recent presentation of crystal structures of anthrax toxin protective antigen, in both monomeric and heptameric forms, is the latest in a recent flurry of pore-forming protein toxin structures. These structures are giving us insights into molecular mechanisms of membrane insertion and the architecture of membrane proteins.
With ever stronger magnetic fields, magnetic alignment of proteins and nucleic acids with the magnetic field can now be observed. In such magnetically aligned systems, dipolar couplings no longer average to zero and the residual splittings contain unique information on molecular conformation and possibly mobility.
The electron crystallographic structure of the aquaporin-1 water channel, determined at ∼6Å, reveals that the protein has six transmembrane αhelices forming a trapezoid-like cylinder. There is a branched rod-like structure within the cylinder that traverses the membrane and likely contains at least one α-helix.
The structure of human heparin binding protein reveals that the serine proteinase fold has been used as a scaffold for a multifunctional protein with antibacterial activity, monocyte and T-cell activating properties and endotoxin and heparin binding capacity.
