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NTPases use a metal ion, typically Mg2+, coordinated by a conserved serine or threonine residue, to enable phosphate binding and catalysis. Now cysteine substitutions at the switch 1 motif of different kinesins render them able to use Mn2+ instead of Mg2+, allowing their enzymatic and motor activities to be modulated by the ratio of Mg2+ to Mn2+.
The combination of an F-box domain with a single-domain antibody that recognizes green fluorescent protein (GFP) now allows controlled depletion of GFP fusions in mammalian cells and in flies. This system, called deGradFP, should be widely useful, as GFP fusions are available for many proteins in model organisms.
The interaction of solvent with protein has been a major unresolved and significant problem for decades. Now, NMR techniques characterize the hydration sites of ubiquitin encapsulated within reverse micelles. This approach reveals a clustering of water molecules with similar residence times, an observation that is generally not accessible by crystallographic analyses.
