Ambidextrous Helical Nanotubes from Self-Assembly of Designed Helical Hairpin Motifs

Hughes, Spencer; Wall, Joseph; Wang, Fengbin; Wang, Shengyuan; Kreutzberger, Mark; Osinski, Tomasz; Orlova, Albina; Zuo, Xiaobing; Egelman, Edward; Conticello, Vincent

doi:10.1073/pnas.1903910116

Title: Ambidextrous Helical Nanotubes from Self-Assembly of Designed Helical Hairpin Motifs

Journal Article · Mon Jul 01 00:00:00 EDT 2019 · Proceedings of the National Academy of Sciences of the United States of America

DOI:https://doi.org/10.1073/pnas.1903910116· OSTI ID:1525381

Hughes, Spencer ^[1]; Wall, Joseph ^[2]; Wang, Fengbin ^[3]; Wang, Shengyuan ^[1]; Kreutzberger, Mark ^[3]; Osinski, Tomasz ^[3]; Orlova, Albina ^[3]; Zuo, Xiaobing ^[4]; Egelman, Edward ^[3]; Conticello, Vincent ^[1]

Emory Univ., Atlanta, GA (United States)
Brookhaven National Lab. (BNL), Upton, NY (United States)
Univ. of Virginia, Charlottesville, VA (United States)
Argonne National Lab. (ANL), Argonne, IL (United States)

Tandem repeat proteins exhibit native designability and represent potentially useful scaffolds for the construction of synthetic biomimetic assemblies. We have designed 2 synthetic peptides, HEAT_R1 and LRV_M3Δ1, based on the consensus sequences of single repeats of thermophilic HEAT (PBS_HEAT) and Leucine-Rich Variant (LRV) structural motifs, respectively. Self-assembly of the peptides afforded high-aspect ratio helical nanotubes. Cryo-electron microscopy with direct electron detection was employed to analyze the structures of the solvated filaments. The 3D reconstructions from the cryo-EM maps led to atomic models for the HEAT_R1 and LRV_M3Δ1 filaments at resolutions of 6.0 and 4.4 Å, respectively. Surprisingly, despite sequence similarity at the lateral packing interface, HEAT_R1 and LRV_M3Δ1 filaments adopt the opposite helical hand and differ significantly in helical geometry, while retaining a local conformation similar to previously characterized repeat proteins of the same class. The differences in the 2 filaments could be rationalized on the basis of differences in cohesive interactions at the lateral and axial interfaces. These structural data reinforce previous observations regarding the structural plasticity of helical protein assemblies and the need for high-resolution structural analysis. Despite these observations, the native designability of tandem repeat proteins offers the opportunity to engineer novel helical nanotubes. Moreover, the resultant nanotubes have independently addressable and chemically distinguishable interior and exterior surfaces that would facilitate applications in selective recognition, transport, and release.

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Research Organization:: Brookhaven National Laboratory (BNL), Upton, NY (United States); Argonne National Laboratory (ANL), Argonne, IL (United States)

Sponsoring Organization:: USDOE Office of Science (SC), Biological and Environmental Research (BER); National Institutes of Health (NIH); National Science Foundation (NSF)

Grant/Contract Number:: SC0012704; AC02-06CH11357

OSTI ID:: 1525381

Alternate ID(s):: OSTI ID: 1563920

Report Number(s):: BNL-211762-2019-JAAM

Journal Information:: Proceedings of the National Academy of Sciences of the United States of America, Vol. 116, Issue 29; ISSN 0027-8424

Publisher:: National Academy of Sciences, Washington, DC (United States)Copyright Statement

Country of Publication:: United States

Language:: English

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Cited by: 27 works

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59 BASIC BIOLOGICAL SCIENCES
Tandem Repeat Proteins
Cryo-EM
Helical Nanotube
Self-Assembly
cryo-EM
helical nanotube
self-assembly
tandem repeat proteins

Title: Ambidextrous Helical Nanotubes from Self-Assembly of Designed Helical Hairpin Motifs

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