Literature DB >> 31182277

Structural diversity of coiled coils in protein fibers of the bacterial cell envelope.

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.
Copyright © 2019 Elsevier GmbH. All rights reserved.

Keywords:  Coiled coil; Polar core; Trimeric autotransporter adhesin; β-layer

Mesh:

Substances:

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


  1 in total

1.  New β-Propellers Are Continuously Amplified From Single Blades in all Major Lineages of the β-Propeller Superfamily.

Authors:  Joana Pereira; Andrei N Lupas
Journal:  Front Mol Biosci       Date:  2022-06-09
  1 in total

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