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Recent structural studies of acetyl-coenzyme A synthase/carbon monoxide dehydrogenase from Moorella thermoacetica revealed a unique Cu-Ni-[Fe4-S4] active site. New data now indicate that active enzyme contains a Ni-Ni-[Fe4-S4] site. Novel chemistry is posited for the central Ni atom of this enzyme, which utilizes the toxic gas CO as a catalytic intermediate.
New structural analysis finds a metal-oxo clusters bound to the iron trafficking protein Fbp. Does this point to a possible strategy for bacterial iron acquisition?
Covalent attachment of ubiquitin-like proteins to other proteins drives numerous important physiological processes. The recent structure of an ubiquitin-like E1 enzyme provides insight into the curious assembly line–like mechanism that initiates all ubiquitin-related protein processing pathways.
Function analysis of 'insulators' has led to the idea that they comprise two separable and mechanistically distinct insulating activities — one blocking enhancer cross-talk and the other barring heterochromatin spreading. However, results from two recent studies have blurred this mechanistic distinction.
Many different RNA species undergo nucleotide modifications at sites identified by guide small nucleolar ribonucleoprotein (snoRNP) particles. The co-crystal structure of two snoRNP proteins gives valuable clues into the workings of this system.