| Literature DB >> 31182277 |
Birte Hernandez Alvarez1, Jens Bassler2, Andrei N Lupas3.
Abstract
The cell envelope of bacteria shows great diversity in architecture and composition, to a large extent due to its proteome. Proteins localized to the cell envelope, whether integrally embedded in the membrane, membrane-anchored, or peripherally associated as part of a macromolecular complex, often form elongated fibers, in which coiled coils represent a prominent structural element. These coiled-coil segments show a surprising degree of structural variability, despite being shaped by a small number of simple biophysical rules, foremost being their geometry of interaction referred to as 'knobs-into-holes'. Here we will review this diversity, particularly as it has emerged over the last decade.Keywords: Coiled coil; Polar core; Trimeric autotransporter adhesin; β-layer
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Year: 2019 PMID: 31182277 DOI: 10.1016/j.ijmm.2019.05.011
Source DB: PubMed Journal: Int J Med Microbiol ISSN: 1438-4221 Impact factor: 3.473