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The solutiuon structure of the GAGA DMA-binding domain reveals an N-terminally extended zinc finger structure which wraps around one turn of the DNA, a result which helps to set limits on the mechanism of nucleosome remodelling.
Two recent crystal structures show channel-forming bacterial toxins as soluble monomers (colicin la) or transmembrane pores (α-haemolysin). Together with other data, these structures imply that toxin activity requires dramatic conformational changes.
A recent Rinshoken conference featuring adgerents of both X-ray crystallography and NMR emphasized the need for using a combination of approaches to solve the sturctures of large molecules.
Protein structure of prediction methods, critically assessed at Asilomar, California, are starting to work, combining ideas descended from two lines of thought: from Darwin and from Boltzmann and Schrodinger.
The crystal structure of a PNA duplex reveals both a right- and a left-handed helix in the unit cell. The helices are wide (28 Å), large pitched (18 bp) with the base pairs perpendicular to the helix axis, thereby demonstrating that PNA besides adapting to oligonucleotide partners also has a unique structure by itself.
The RecA protein forms a hexameric ring that is similar to the core of the F1-ATPase. Several lines of evidence suggest that this hexamer may be a structural homologue of ring helicases.
The high resolution structure of the new therapeutic target, cathepsin K, complexed with the potent mechanism-based inhibitor, APC3328, reveals the substrate-binding sites of this cysteine proteinase and validates the binding mode for this inhibitor class.
The structure of human cathepsin K, a potential target for treatment of osteoporosis, reveals active site differences with homologous cysteine proteinases that should enable the design of cathepsin K selective inhibitors.
Kinetic and spectroscopic evidence show that certain bZIP peptides favour a DMA binding mechanism in which monomers sequentially assemble into a dimer at their DMA target site.
The three-dimensional structure of actively transcribing rotavirus particles reveals that the nascent mRNA transcripts generated within the core of the virion by endogenous transcriptase complexes are translocated through the intact capsid through a system of channels at the icosahedral five-fold axes.
