Microbial βγ-crystallins

Prog Biophys Mol Biol. 2014 Jul;115(1):42-51. doi: 10.1016/j.pbiomolbio.2014.02.007. Epub 2014 Mar 1.

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.

Keywords: Ca(2+)-binding; Evolution; Greek key motif; Microbial relatives; βγ Domain; βγ-Crystallins.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Amino Acid Motifs
  • Amino Acid Sequence
  • Animals
  • Humans
  • Microbiology*
  • Molecular Sequence Data
  • Protein Stability
  • Protein Structure, Tertiary
  • beta-Crystallins* / chemistry
  • beta-Crystallins* / metabolism
  • gamma-Crystallins* / chemistry
  • gamma-Crystallins* / metabolism

Substances

  • beta-Crystallins
  • gamma-Crystallins