The UlaG protein family defines novel structural and functional motifs grafted on an ancient RNase fold.

ABSTRACT:

Background

Bacterial populations are highly successful at colonizing new habitats and adapting to changing environmental conditions, partly due to their capacity to evolve novel virulence and metabolic pathways in response to stress conditions and to shuffle them by horizontal gene transfer (HGT). A common theme in the evolution of new functions consists of gene duplication followed by functional divergence. UlaG, a unique manganese-dependent metallo-β-lactamase (MBL) enzyme involved in L-ascorbate metabolism by commensal and symbiotic enterobacteria, provides a model for the study of the emergence of new catalytic activities from the modification of an ancient fold. Furthermore, UlaG is the founding member of the so-called UlaG-like (UlaGL) protein family, a recently established a

SUBMITTER: Fernandez FJ 

PROVIDER: S-EPMC3219644 | biostudies-literature | 2011 Sep

REPOSITORIES: biostudies-literature