Structure and topology of the linkers in the conserved lepidosaur β-keratin chain with four 34-residue repeats support an interfilament role for the central linker
•The 20 topologies of the four 34-residue repeats and the three linkers are described.•A serine-X dipeptide repeat occurs in the central linker only.•A beta-sandwich in neighbouring filaments is connected by the central linker. The β-keratin chain with four 34-residue repeats that is conserved acros...
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| Published in | Journal of structural biology Vol. 212; no. 1; p. 107599 |
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| Format | Journal Article |
| Language | English |
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01.10.2020
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| Abstract | •The 20 topologies of the four 34-residue repeats and the three linkers are described.•A serine-X dipeptide repeat occurs in the central linker only.•A beta-sandwich in neighbouring filaments is connected by the central linker.
The β-keratin chain with four 34-residue repeats that is conserved across the lepidosaurs (lizards, snakes and tuatara) contains three linker regions as well as a short, conserved N-terminal domain and a longer, more variable C-terminal domain. Earlier modelling had shown that only six classes of structure involving the four 34-residue repeats were possible. In three of these the 34-residue repeats were confined to a single filament (Classes 1, 2 and 3) whereas in the remaining three classes the repeats lay in two, three or four filaments, with some of the linkers forming interfilament connections (Classes 4, 5 and 6). In this work the members of each class of structure (a total of 20 arrangements) have been described and a comparison has been made of the topologies of each of the linker regions. This provides new constraints on the structure of the chain as a whole. Also, analysis of the sequences of the three linker regions has revealed that the central linker (and only the central linker) contains four short regions displaying a distinctive dipeptide repeat of the form (S-X)2,3 separated by short regions containing proline and cysteine residues. By analogy with silk fibroin proteins this has the capability of forming a β-sheet-like conformation. Using the topology and sequence data the evidence suggests that the four 34-residue repeat chain adopts a Class 4a structure with a β-sandwich in filament 1 connected through the central linker to a β-sandwich in filament 2. |
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| AbstractList | The β-keratin chain with four 34-residue repeats that is conserved across the lepidosaurs (lizards, snakes and tuatara) contains three linker regions as well as a short, conserved N-terminal domain and a longer, more variable C-terminal domain. Earlier modelling had shown that only six classes of structure involving the four 34-residue repeats were possible. In three of these the 34-residue repeats were confined to a single filament (Classes 1, 2 and 3) whereas in the remaining three classes the repeats lay in two, three or four filaments, with some of the linkers forming interfilament connections (Classes 4, 5 and 6). In this work the members of each class of structure (a total of 20 arrangements) have been described and a comparison has been made of the topologies of each of the linker regions. This provides new constraints on the structure of the chain as a whole. Also, analysis of the sequences of the three linker regions has revealed that the central linker (and only the central linker) contains four short regions displaying a distinctive dipeptide repeat of the form (S-X)
separated by short regions containing proline and cysteine residues. By analogy with silk fibroin proteins this has the capability of forming a β-sheet-like conformation. Using the topology and sequence data the evidence suggests that the four 34-residue repeat chain adopts a Class 4a structure with a β-sandwich in filament 1 connected through the central linker to a β-sandwich in filament 2. •The 20 topologies of the four 34-residue repeats and the three linkers are described.•A serine-X dipeptide repeat occurs in the central linker only.•A beta-sandwich in neighbouring filaments is connected by the central linker. The β-keratin chain with four 34-residue repeats that is conserved across the lepidosaurs (lizards, snakes and tuatara) contains three linker regions as well as a short, conserved N-terminal domain and a longer, more variable C-terminal domain. Earlier modelling had shown that only six classes of structure involving the four 34-residue repeats were possible. In three of these the 34-residue repeats were confined to a single filament (Classes 1, 2 and 3) whereas in the remaining three classes the repeats lay in two, three or four filaments, with some of the linkers forming interfilament connections (Classes 4, 5 and 6). In this work the members of each class of structure (a total of 20 arrangements) have been described and a comparison has been made of the topologies of each of the linker regions. This provides new constraints on the structure of the chain as a whole. Also, analysis of the sequences of the three linker regions has revealed that the central linker (and only the central linker) contains four short regions displaying a distinctive dipeptide repeat of the form (S-X)2,3 separated by short regions containing proline and cysteine residues. By analogy with silk fibroin proteins this has the capability of forming a β-sheet-like conformation. Using the topology and sequence data the evidence suggests that the four 34-residue repeat chain adopts a Class 4a structure with a β-sandwich in filament 1 connected through the central linker to a β-sandwich in filament 2. |
| ArticleNumber | 107599 |
| Author | Parry, David A.D. |
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| CitedBy_id | crossref_primary_10_1016_j_foodchem_2023_135854 crossref_primary_10_1016_j_ydbio_2023_05_007 crossref_primary_10_1016_j_jsb_2021_107793 crossref_primary_10_3390_genes12040591 |
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| Keywords | Serine repeat motif Topology of repeats and linkers β-Keratin Lepidosaurs |
| Language | English |
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| Snippet | •The 20 topologies of the four 34-residue repeats and the three linkers are described.•A serine-X dipeptide repeat occurs in the central linker only.•A... The β-keratin chain with four 34-residue repeats that is conserved across the lepidosaurs (lizards, snakes and tuatara) contains three linker regions as well... |
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| SubjectTerms | Lepidosaurs Serine repeat motif Topology of repeats and linkers β-Keratin |
| Title | Structure and topology of the linkers in the conserved lepidosaur β-keratin chain with four 34-residue repeats support an interfilament role for the central linker |
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