β‐Rolls, β‐Helices, and Other β‐Solenoid Proteins

Kajava, Andrey V.; Steven, Alasdair C.

doi:10.1016/s0065-3233(06)73003-0

Cited by 149Protein Structure and DynamicsEnzyme Structure and FunctionBiochemical and Structural Characterization

β‐Rolls, β‐Helices, and Other β‐Solenoid Proteins

Kajava, Andrey V., Steven, Alasdair C.·2006·Advances in Protein Chemistry

DOI 10.1016/s0065-3233(06)73003-0

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Abstract

Beta-rolls and beta-helices belong to a larger group of topologically similar proteins with solenoid folds: because their regular secondary structure elements are exclusively beta-strands, they are referred to as beta-solenoids. The number of beta-solenoids whose structures are known is now large enough to support a systematic analysis. Here we survey the distinguishing structural features of beta-solenoids, also documenting their notable diversity. Appraisal of these structures suggests a classification based on handedness, twist, oligomerization state, and coil shape. In addition, beta-solenoids are distinguished by the number of chains that wind around a common axis: the majority are single-stranded but there is a recently discovered subset of triple-stranded beta-solenoids. This survey has revealed some relationships of the amino acid sequences of beta-solenoids with their structures and functions-in particular, the repetitive character of the coil sequences and conformations that recur in tracts of tandem repeats. We have proposed the term beta-arc for the distinctive turns found in beta-solenoids and beta-arch for the corresponding strand-turn-strand motifs. The evolutionary mechanisms underlying these proteins are also discussed. This analysis has direct implications for sequence-based detection, structural prediction, and de novo design of other beta-solenoid proteins. The abundance of virulence factors, toxins and allergens among beta-solenoids, as well as commonalities of beta-solenoids with amyloid fibrils, imply that this class of folds may have a broader role in human diseases than was previously recognized. Thus, identification of genes with putative beta-solenoid domains promises to be a fertile direction in the search for viable targets in the development of new antibiotics and vaccines.

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Tandem repeat proteins with repetitive units of 6-10 residues predominantly have beta-solenoid structures.
“Tandem repeat proteins with repetitive units of 6–10 residues predominantly have beta-solenoid structures25.”
From A structural biology community assessment of AlphaFold2 applications (2022) · cites this paper as [25]

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Authors: Kajava, A. V., & Steven, A. C.
Affiliations: Centre National de la Recherche Scientifique (FR)
National Institutes of Health (US)
ORCID: Kajava, Andrey V.
Steven, Alasdair C.
Venue: Advances in Protein Chemistry
Publisher: Elsevier
Published: 2006
Volume: 73
Pages: 55-96
ISSN: 0065-3233 (ISSN-L)
DOI: 10.1016/s0065-3233(06)73003-0
OpenAlex: W133512539
Cited by: 149
References: 108
Citations by year: 2026: 5 · 2025: 10 · 2024: 10 · 2023: 10 · 2022: 8 · 2021: 7 · 2020: 5 · 2019: 4 · 2018: 7 · 2017: 12 · 2016: 12 · 2015: 8 · 2014: 7 · 2013: 12 · 2012: 4
FWCI: 10.02
Type: book chapter
Language: en
Open access: closed
Locations: Advances in protein chemistry (publishedVersion)
PubMed (publishedVersion)
Funders: National Institutes of Health
National Institute of Arthritis and Musculoskeletal and Skin Diseases
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Structural Characterization
Keywords: beta-helix, protein fold classification, oligomeric state, tandem repeats, protein evolution, virulence factors, toxins, allergens, amyloid fibrils, de novo protein design, antibiotic targets, vaccine targets
MeSH terms: Models, Molecular, Proteins, Protein Structure, Secondary, Protein Folding

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β‐Rolls, β‐Helices, and Other β‐Solenoid Proteins

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