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Int Rev Cell Mol Biol. 2014;308:1-34. doi: 10.1016/B978-0-12-800097-7.00001-4.

Structure and function of POTRA domains of Omp85/TPS superfamily.

Author information

1
Department of Biochemistry and Cellular and Molecular Biology, Knoxville, Tennessee, USA.
2
Department of Biochemistry and Cellular and Molecular Biology, Knoxville, Tennessee, USA; Department of Microbiology, University of Tennessee, Knoxville, Tennessee, USA. Electronic address: bbruce@utk.edu.

Abstract

The Omp85/TPS (outer-membrane protein of 85 kDa/two-partner secretion) superfamily is a ubiquitous and major class of β-barrel proteins. This superfamily is restricted to the outer membranes of gram-negative bacteria, mitochondria, and chloroplasts. The common architecture, with an N-terminus consisting of repeats of soluble polypeptide-transport-associated (POTRA) domains and a C-terminal β-barrel pore is highly conserved. The structures of multiple POTRA domains and one full-length TPS protein have been solved, yet discovering roles of individual POTRA domains has been difficult. This review focuses on similarities and differences between POTRA structures, emphasizing POTRA domains in autotrophic organisms including plants and cyanobacteria. Unique roles, specific for certain POTRA domains, are examined in the context of POTRA location with respect to their attachment to the β-barrel pore, and their degree of biological dispensability. Finally, because many POTRA domains may have the ability to interact with thousands of partner proteins, possible modes of these interactions are also explored.

KEYWORDS:

Outer-membrane protein 85kDa; Polypeptide-transport-associated; Toc75; Two-partner secretion

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