| Literature DB >> 15866036 |
Shane E Cotter1, Neeraj K Surana, Joseph W St Geme.
Abstract
Autotransporter proteins are a large family of gram-negative bacterial extracellular proteins. These proteins have a characteristic arrangement of functional domains, including an N-terminal signal peptide, an internal passenger domain, and a C-terminal translocator domain. Recent studies have identified a novel subfamily of autotransporters, defined by a short trimeric C-terminal translocator domain and known as trimeric autotransporters. In this article, we review our current knowledge of the structural and functional characteristics of trimeric autotransporters, highlighting the distinctions between this subfamily and conventional autotransporters. We speculate that trimeric autotransporters evolved to enable high-affinity multivalent adhesive interactions with host surfaces and circulating host molecules to take place.Mesh:
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Year: 2005 PMID: 15866036 DOI: 10.1016/j.tim.2005.03.004
Source DB: PubMed Journal: Trends Microbiol ISSN: 0966-842X Impact factor: 17.079