Association properties and unfolding of a βγ-crystallin domain of a Vibrio-specific protein.

ABSTRACT: The βγ-crystallin superfamily possesses a large number of versatile members, of which only a few members other than lens βγ-crystallins have been studied. Understanding the non-crystallin functions as well as origin of crystallin-like properties of such proteins is possible by exploring novel members from diverse sources. We describe a novel βγ-crystallin domain with S-type (Spherulin 3a type) Greek key motifs in protein vibrillin from a pathogenic bacterium Vibrio cholerae. This domain is a part of a large Vibrio-specific protein prevalent in Vibrio species (found in at least fourteen different strains sequenced so far). The domain contains two canonical N/D-N/D-X-X-S/T-S Ca(2+)-binding motifs, and bind Ca(2+). Unlike spherulin 3a and other microbial homologues studied so far, βγ-crystall

SUBMITTER: Suman SK 

PROVIDER: S-EPMC3551895 | biostudies-literature | 2013

REPOSITORIES: biostudies-literature