Article Abstract:
The crystal structure of the mutagenic protein UmuD of Escherichia coli at 2.5 angstrom resolution reveals globular heads folded in a rare beta-structure that cohere to form dimer molecules. The extended amino-acid tail congregate to form crystallized filaments. UmuD filament forms a scaffold on the RecA-DNA filament that places UmuC efficiently for interaction with DNA polymerase III holoenzyme. Analysis of the structure indicates that UmuD undergoes self-cleavage reactions during the global SOS response.
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Article Abstract:
The 2.9-angstrom-resolution structure of a partially deglycosylated complex of human follicle-stimulating hormone (FSH) bound to the extracellular hormone-binding domain of its receptor (FSHR(sub HB)) is presented. The analysis suggests that all glycoprotein hormones bind to their receptors in this mode and that binding specificity is mediated by key interaction sites both the common alpha- and hormone-specific beta-subunits
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Article Abstract:
The crystal structure of a calcium-dependent animal lectin, a type of mannose-binding carbohydrate recognition protein, shows the role of calcium ions in binding. The structure also sheds light on why these proteins bind some sugars and not others. For example, two oligosaccharide branches crosslink with the crystal to allow multivalent binding of one oligosaccharide chain.
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