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TitleStructural analysis of cross α-helical nanotubes provides insight into the designability of filamentous peptide nanomaterials.
Journal, issue, pagesNat Commun, Vol. 12, Issue 1, Page 407, Year 2021
Publish dateJan 18, 2021
AuthorsFengbin Wang / Ordy Gnewou / Charles Modlin / Leticia C Beltran / Chunfu Xu / Zhangli Su / Puneet Juneja / Gevorg Grigoryan / Edward H Egelman / Vincent P Conticello /
PubMed AbstractThe exquisite structure-function correlations observed in filamentous protein assemblies provide a paradigm for the design of synthetic peptide-based nanomaterials. However, the plasticity of ...The exquisite structure-function correlations observed in filamentous protein assemblies provide a paradigm for the design of synthetic peptide-based nanomaterials. However, the plasticity of quaternary structure in sequence-space and the lability of helical symmetry present significant challenges to the de novo design and structural analysis of such filaments. Here, we describe a rational approach to design self-assembling peptide nanotubes based on controlling lateral interactions between protofilaments having an unusual cross-α supramolecular architecture. Near-atomic resolution cryo-EM structural analysis of seven designed nanotubes provides insight into the designability of interfaces within these synthetic peptide assemblies and identifies a non-native structural interaction based on a pair of arginine residues. This arginine clasp motif can robustly mediate cohesive interactions between protofilaments within the cross-α nanotubes. The structure of the resultant assemblies can be controlled through the sequence and length of the peptide subunits, which generates synthetic peptide filaments of similar dimensions to flagella and pili.
External linksNat Commun / PubMed:33462223 / PubMed Central
MethodsEM (helical sym.)
Resolution3.8 - 4.4 Å
Structure data

21812

6wkx

EMDB-21812, PDB-6wkx:
Cryo-EM of Form 1 related peptide filament, 15-10-3
Method: EM (helical sym.) / Resolution: 4.2 Å

21813

6wky

EMDB-21813, PDB-6wky:
Cryo-EM of Form 1 related peptide filament, 29-24-3
Method: EM (helical sym.) / Resolution: 4.2 Å

21814

6wl0

EMDB-21814, PDB-6wl0:
Cryo-EM of Form 1 related peptide filament, 36-31-3-RD
Method: EM (helical sym.) / Resolution: 4.4 Å

21815

6wl1

EMDB-21815, PDB-6wl1:
Cryo-EM of Form 1 related peptide filament, 36-31-3
Method: EM (helical sym.) / Resolution: 4.0 Å

21816

6wl7

EMDB-21816, PDB-6wl7:
Cryo-EM of Form 2 like peptide filament, 29-20-2
Method: EM (helical sym.) / Resolution: 3.8 Å

21817

6wl8

EMDB-21817, PDB-6wl8:
Cryo-EM of Form 2 peptide filament
Method: EM (helical sym.) / Resolution: 4.1 Å

21818

6wl9

EMDB-21818, PDB-6wl9:
Cryo-EM of Form 2 like peptide filament, Form2a
Method: EM (helical sym.) / Resolution: 4.2 Å

Source
  • synthetic construct (others)
KeywordsPROTEIN FIBRIL / filament / self-assembly peptide filament / Cryo-EM

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