title: Microbial βγ-crystallins.
abstract: 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 Ca(2+)-binding proteins with huge diversity. The βγ domain shows variable properties in Ca(2+) 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.
authors.affiliation: CSIR - Centre for Cellular and Molecular Biology (CCMB), Uppal Road, Hyderabad 500 007, India.
authors.forename: Amita
authors.initials: A
authors.lastname: Mishra
authors.affiliation: CSIR - Centre for Cellular and Molecular Biology (CCMB), Uppal Road, Hyderabad 500 007, India.
authors.forename: Bal
authors.initials: B
authors.lastname: Krishnan
authors.affiliation: CSIR - Centre for Cellular and Molecular Biology (CCMB), Uppal Road, Hyderabad 500 007, India.
authors.forename: Shanti Swaroop
authors.initials: SS
authors.lastname: Srivastava
authors.affiliation: CSIR - Centre for Cellular and Molecular Biology (CCMB), Uppal Road, Hyderabad 500 007, India. Electronic address: yogendra@ccmb.res.in.
authors.forename: Yogendra
authors.initials: Y
authors.lastname: Sharma
mesh_terms: D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D000818:Animals; D006801:Humans; D008829:Microbiology; D008969:Molecular Sequence Data; D055550:Protein Stability; D017434:Protein Structure, Tertiary; D038204:beta-Crystallins / Q000737:chemistry / Q000378:metabolism; D038222:gamma-Crystallins / Q000737:chemistry / Q000378:metabolism
chemical_list: D038204:beta-Crystallins; D038222:gamma-Crystallins
keywords: Ca(2+)-binding; Evolution; Greek key motif; Microbial relatives; βγ Domain; βγ-Crystallins