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The crystal structure of l-Crel offers the first view of an intron-encoded endonuclease. The structure differs from known endonuclease structures, revealing an elongated saddle shaped molecule ideally suited for binding a long DNA sequence.
The chemistry of sulphur enables a disulphide bond to be transitory—guiding the proper folding of a protein, but not appearing in the native structure.
Structures of the catalytic domains of λ, Int and HP1 integrase provide insight into the diversity of the Int family of recombinases, which nevertheless catalyse very similar chemical events.
Recently, the crystal structure of the N-terminal fragment of human Hsp90-alpha chaperone and its complex with geldanamycin and the crystal structure of the N-terminal domain of yeast Hsp90 have been determined at high resolution. These structures reveal features that shed new light on the Hsp90 chaperone–protein interactions.
The crystal structure of glial cell-derived neurotrophic factor (GDNF) reveals two independent copies of the dimer that differ significantly through a hinge bending at the central, disulphide-rich region. GDNF is compared with other members of the TGF-β family, and potential receptor binding surfaces are identified.
Coagulation factors IX/X-binding protein is an intertwined dimer with a central loop projecting into the adjoining subunit. Excluding this loop, each subunit has a fold similar to rat mannose-binding protein.
