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Curr Opin Struct Biol. 1997 Jun;7(3):407-15.

Modular multidomain phosphoryl transfer proteins of bacteria.

Author information

1
Department of Biology, University of California at San Diego, La Jolla, 92093-0116, USA. jreizer@ucad.edu

Abstract

Recent phylogenetic and structural analyses of multidomain phosphoryl transfer proteins of bacteria have revealed that interdomain (but not intradomain) splicing and fusion, as well as domain duplication and deletion, have occurred frequently during evolution. These events have been found to be exceedingly rare in certain other protein families. Domain-shuffling events are illustrated by examples from the superfamilies of phosphoenolpyruvate-dependent sugar phosphotransferase systems, their transcriptional regulatory protein targets of phosphorylation, sensor autokinase/response regulator signal transduction systems, and permeases of the ATP-binding-cassette type.

PMID:
9204284
[Indexed for MEDLINE]

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