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The βγ-crystallin superfamily consists of a class of homologous two-domain proteins with Greek-key fold. Protein S, a Ca 2+ -binding spore-coat protein from the soil bacterium Myxococcus xanthus exhibits a high degree of sequential and structural homology with γB-crystallin from the vertebrate eye lens. In contrast to γB-crystallin, which undergoes irreversible aggregation upon thermal...
Protein S, a two-domain spore coat protein from Myxococcus xanthus, is structurally related to eye-lens βγ-crystallins. No natural monomeric one-domain member of this protein superfamily is known. To determine the stability of the single domains and to explain the ubiquitous domain duplication, the isolated domains of protein S were constructed. The N-domain is thermodynamically more stable than the...
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