Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2070003 | Progress in Biophysics and Molecular Biology | 2014 | 10 Pages |
βγ-Crystallins have emerged as a superfamily of structurally homologous proteins with representatives across the domains of life. A major portion of this superfamily is constituted by members from microorganisms. This superfamily has also been recognized as a novel group of Ca2+-binding proteins with huge diversity. The βγ domain shows variable properties in Ca2+ binding, stability and association with other domains. The various members present a series of evolutionary adaptations culminating in great diversity in properties and functions. Most of the predicted βγ-crystallins are yet to be characterized experimentally. In this review, we outline the distinctive features of microbial βγ-crystallins and their position in the βγ-crystallin superfamily.