Unknown

Dataset Information

0

A topologically diverse family of fluoride channels.


ABSTRACT: Dual-topology proteins are likely evolutionary antecedents to a common motif in membrane protein structures, the inverted repeat. A family of fluoride channels, the Flucs, which protect microorganisms, fungi, and plants against cytoplasmic fluoride accumulation, has representatives of all topologies along this evolutionary trajectory, including dual-topology homodimers, antiparallel heterodimers, and, in eukaryotes, fused two-domain proteins with an inverted repeat motif. Recent high-resolution crystal structures of dual-topology homodimers, coupled with extensive functional information about both the homodimers and two-domain Flucs, provide a case study of the co-evolution of fold and function.

SUBMITTER: Macdonald CB 

PROVIDER: S-EPMC5612848 | biostudies-literature | 2017 Aug

REPOSITORIES: biostudies-literature

altmetric image

Publications

A topologically diverse family of fluoride channels.

Macdonald Christian B CB   Stockbridge Randy B RB  

Current opinion in structural biology 20170514


Dual-topology proteins are likely evolutionary antecedents to a common motif in membrane protein structures, the inverted repeat. A family of fluoride channels, the Flucs, which protect microorganisms, fungi, and plants against cytoplasmic fluoride accumulation, has representatives of all topologies along this evolutionary trajectory, including dual-topology homodimers, antiparallel heterodimers, and, in eukaryotes, fused two-domain proteins with an inverted repeat motif. Recent high-resolution  ...[more]

Similar Datasets

| S-EPMC8315801 | biostudies-literature
| S-EPMC7054162 | biostudies-literature
| S-EPMC3683667 | biostudies-literature
| S-EPMC5900737 | biostudies-literature
| S-EPMC4839437 | biostudies-literature
| S-EPMC3839697 | biostudies-literature
| S-EPMC6419456 | biostudies-literature
| S-EPMC5884710 | biostudies-literature
| S-EPMC4766968 | biostudies-literature
| S-EPMC1302145 | biostudies-other