scholarly journals Structural diversity of oligomeric β-propellers with different numbers of identical blades

eLife ◽  
2019 ◽  
Vol 8 ◽  
Author(s):  
Evgenia Afanasieva ◽  
Indronil Chaudhuri ◽  
Jörg Martin ◽  
Eva Hertle ◽  
Astrid Ursinus ◽  
...  
Keyword(s):  
High Resolution ◽  
Building Block ◽  
Polypeptide Chain ◽  
Structural Diversity ◽  
Building Blocks ◽  
Single Chain ◽  
Single Polypeptide Chain ◽  
Data Support ◽  
Single Polypeptide ◽  
Structural Versatility

β-Propellers arise through the amplification of a supersecondary structure element called a blade. This process produces toroids of between four and twelve repeats, which are almost always arranged sequentially in a single polypeptide chain. We found that new propellers evolve continuously by amplification from single blades. We therefore investigated whether such nascent propellers can fold as homo-oligomers before they have been fully amplified within a single chain. One- to six-bladed building blocks derived from two seven-bladed WD40 propellers yielded stable homo-oligomers with six to nine blades, depending on the size of the building block. High-resolution structures for tetramers of two blades, trimers of three blades, and dimers of four and five blades, respectively, show structurally diverse propellers and include a novel fold, highlighting the inherent flexibility of the WD40 blade. Our data support the hypothesis that subdomain-sized fragments can provide structural versatility in the evolution of new proteins.

scholarly journals Structural diversity of oligomeric β-propellers with different numbers of identical blades

2019 ◽  
Author(s):  
Evgenia Afanasieva ◽  
Indronil Chaudhuri ◽  
Jörg Martin ◽  
Eva Hertle ◽  
Astrid Ursinus ◽  
...  
Keyword(s):  
High Resolution ◽  
Building Block ◽  
Polypeptide Chain ◽  
Structural Diversity ◽  
Building Blocks ◽  
Single Chain ◽  
Single Polypeptide Chain ◽  
Data Support ◽  
Single Polypeptide ◽  
Structural Versatility

Abstractβ-Propellers arise through the amplification of a supersecondary structure element called a blade. This process produces toroids of between four and twelve repeats, which are almost always arranged sequentially in a single polypeptide chain. We found that new propellers evolve continuously by amplification from single blades. We therefore investigated whether such nascent propellers can fold as homo-oligomers before they have been fully amplified within a single chain. One-to six-bladed building blocks derived from two seven-bladed WD40 propellers yielded stable homo-oligomers with six to nine blades, depending on the size of the building block. High-resolution structures for tetramers of two blades, trimers of three blades, and dimers of four and five blades, respectively, show structurally diverse propellers and include a novel fold, highlighting the inherent flexibility of the WD40 blade. Our data support the hypothesis that subdomain-sized fragments can provide structural versatility in the evolution of new proteins.

scholarly journals Tetravalent single-chain avidin: from subunits to protein domains via circularly permuted avidins

2005 ◽  
Vol 392 (3) ◽  
pp. 485-491 ◽  
Author(s):  
Henri R. Nordlund ◽  
Vesa P. Hytönen ◽  
Jarno Hörhä ◽  
Juha A. E. Määttä ◽  
Daniel J. White ◽  
...  
Keyword(s):  
Binding Sites ◽  
Polypeptide Chain ◽  
Protein Complexes ◽  
Fusion Partner ◽  
Wild Type ◽  
Single Chain ◽  
Binding Domains ◽  
Single Polypeptide Chain ◽  
Biotin Binding ◽  
Single Polypeptide

scAvd (single-chain avidin, where two dcAvd are joined in a single polypeptide chain), having four biotin-binding domains, was constructed by fusion of topologically modified avidin units. scAvd showed similar biotin binding and thermal stability properties as chicken avidin. The DNA construct encoding scAvd contains four circularly permuted avidin domains, plus short linkers connecting the four domains into a single polypeptide chain. In contrast with wild-type avidin, which contains four identical avidin monomers, scAvd enables each one of the four avidin domains to be independently modified by protein engineering. Therefore the scAvd scaffold can be used to construct spatially and stoichiometrically defined pseudotetrameric avidin molecules showing different domain characteristics. In addition, unmodified scAvd could be used as a fusion partner, since it provides a unique non-oligomeric structure, which is fully functional with four high-affinity biotin-binding sites. Furthermore, the subunit-to-domain strategy described in the present study could be applied to other proteins and protein complexes, facilitating the development of sophisticated protein tools for applications in nanotechnology and life sciences.

Debranching enzyme from rabbit skeletal muscle; Evidence for the location of two active centres on a single polypeptide chain

FEBS Letters ◽  
1975 ◽  
Vol 58 (1-2) ◽  
pp. 181-185 ◽  
Author(s):  
Edna J. Bates ◽  
Gillian M. Heaton ◽  
Carol Taylor ◽  
John C. Kernohan ◽  
Philip Cohen
Keyword(s):  
Skeletal Muscle ◽  
Polypeptide Chain ◽  
Rabbit Skeletal Muscle ◽  
Debranching Enzyme ◽  
Single Polypeptide Chain ◽  
Single Polypeptide ◽  
Active Centres

scholarly journals Hepatic microsomal epoxide hydrase. Chemical evidence for a single polypeptide chain.

1979 ◽  
Vol 254 (14) ◽  
pp. 6240-6243 ◽  
Author(s):  
G C DuBois ◽  
E Appella ◽  
R Armstrong ◽  
W Levin ◽  
A Y Lu ◽  
...  
Keyword(s):  
Polypeptide Chain ◽  
Single Polypeptide Chain ◽  
Single Polypeptide ◽  
Chemical Evidence

scholarly journals Identification of Igh-C-linked determinants on suppressor T cell hybrids and factors specific for L-glutamic acid60-L-alanine30-L-tyrosine10 (GAT).

1985 ◽  
Vol 162 (3) ◽  
pp. 1044-1059 ◽  
Author(s):  
C M Sorensen ◽  
R J Hayashi ◽  
C W Pierce
Keyword(s):  
T Cells ◽  
T Cell ◽  
Polypeptide Chain ◽  
Spleen Cells ◽  
Suppressor T Cell ◽  
Cell Hybrids ◽  
Single Polypeptide Chain ◽  
Functional Classes ◽  
Single Polypeptide ◽  
Ig Allotype

Hyperimmunization of BALB/c mice with concanavalin A-stimulated blasts from the Ig allotype-congenic strain, C.B20, results in the production of antibodies reactive with T cells in an allotype-restricted manner. Spleen cells from these hyperimmune BALB/c mice were used to generate a panel of hybridomas that secrete monoclonal antibodies, reactive, in an allotype-restricted manner, exclusively with T cells subpopulations, and in particular, reactive with suppressor T cell hybridomas and their secreted soluble factors. Two functional classes of antibodies were identified: those that react with single polypeptide-chain suppressor T cell factors (TsF1) and the suppressor T cell hybridomas that produce such factors, and those that react with two polypeptide-chain suppressor T cell factors (TsF2) and their corresponding suppressor T cell hybridomas. These two classes of antibody were used to isolate molecules from the membranes of the respective suppressor T cell hybrids that are functionally and structurally related to the secreted suppressor T cell factors, suggesting a receptor function for these molecules.

The power of the force: mechano-physiology of the giant titin

2018 ◽  
Vol 2 (5) ◽  
pp. 681-686 ◽  
Author(s):  
Jaime Andrés Rivas-Pardo
Keyword(s):  
Amino Acid ◽  
Human Body ◽  
Actin Filaments ◽  
Polypeptide Chain ◽  
Single Gene ◽  
The Other ◽  
Amino Acid Residues ◽  
The Third ◽  
Single Polypeptide Chain ◽  
Single Polypeptide

Titin — the largest protein in the human body — spans half of the muscle sarcomere from the Z-disk to the M-band through a single polypeptide chain. More than 30 000 amino acid residues coded from a single gene (TTN, in humans Q8WZ42) form a long filamentous protein organized in individual globular domains concatenated in tandem. Owing to its location and close interaction with the other muscle filaments, titin is considered the third filament of muscle, after the thick-myosin and the thin-actin filaments.

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