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The first sighting of the ATP synthase ε subunit structure—a vital component of the stalk involved in energy transmission between membrane-bound and cytoplasmic portions of the synthase—provides intriguing hints about its possible mode of action.
Uteroglobin—a small, water soluble homodimeric protein possessing a large interior cavity—encloses a variety of endogenous and xenobiotic hydrophobic molecules. Although the structural results have mechanistic implications, the function of the protein remains speculative.
Analyses of the Alzheimer's disease β-amyloid peptide are revealing the chemical basis for its propensity to form insoluble neurotoxic fibrils and suggest an intriguing link between the free radical theory of neurodegenerative disorders and the chemistry of amyloidogenic peptides.
New structures of copper containing proteins with cupredoxin-like folds confirm earlier predictions, and reveal electron-transfer routes in cytochrome oxidase, while a new fold for amine-oxidase reveals a new use for copper in forming self-derived quino-cofactor.
The crystal structure of the haemopexin-like C-terminal domain of gelatinase A reveals that it is a four-bladed β-propeller protein. The four blades are arranged around a channel-like opening in which Ca2+ and a Na-Cl+ion pair are bound.
Crystal structures of target peptide bound Ca2+-calmodulin linker helix mutants with the helix shortened by two or three residues, or replaced by the longer troponin C central helix, show that the major calmodulin-target structure is preserved at the expense of linker conformation.
The N-terminal domain of fibronectin undergoes factor XIIIa-catalysed crosslinking to fibrin, bacteria and collagen. The reactive glutamine residue is in an extended, random coil ‘tail’ of about 18 residues that would be accessible for crosslinking.
The structure of peptide N-AcYTLDADF when bound to the large subunit of mouse ribonucleotide reductase has been elucidated by transfer NOE. This structure suggests a general design for type 1 RR inhibitors.
