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6VY1

Cryo-EM structure of filamentous PFD from Methanocaldococcus jannaschii

Summary for 6VY1
Entry DOI10.2210/pdb6vy1/pdb
EMDB information21455
DescriptorPrefoldin subunit alpha 2 (1 entity in total)
Functional Keywordshelical symmetry, nanowire, prefoldin, protein fibril
Biological sourceMethanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Total number of polymer chains14
Total formula weight229748.97
Authors
Wang, F.,Chen, Y.X.,Ing, N.L.,Hochbaum, A.I.,Clark, D.S.,Glover, D.J.,Egelman, E.H. (deposition date: 2020-02-25, release date: 2020-05-13, Last modification date: 2025-05-14)
Primary citationChen, Y.X.,Ing, N.L.,Wang, F.,Xu, D.,Sloan, N.B.,Lam, N.T.,Winter, D.L.,Egelman, E.H.,Hochbaum, A.I.,Clark, D.S.,Glover, D.J.
Structural Determination of a Filamentous Chaperone to Fabricate Electronically Conductive Metalloprotein Nanowires.
Acs Nano, 14:6559-6569, 2020
Cited by
PubMed Abstract: The transfer of electrons through protein complexes is central to cellular respiration. Exploiting proteins for charge transfer in a controllable fashion has the potential to revolutionize the integration of biological systems and electronic devices. Here we characterize the structure of an ultrastable protein filament and engineer the filament subunits to create electronically conductive nanowires under aqueous conditions. Cryoelectron microscopy was used to resolve the helical structure of gamma-prefoldin, a filamentous protein from a hyperthermophilic archaeon. Conjugation of tetra-heme c3-type cytochromes along the longitudinal axis of the filament created nanowires capable of long-range electron transfer. Electrochemical transport measurements indicated networks of the nanowires capable of conducting current between electrodes at the redox potential of the cytochromes. Functionalization of these highly engineerable nanowires with other molecules, such as redox enzymes, may be useful for bioelectronic applications.
PubMed: 32347705
DOI: 10.1021/acsnano.9b09405
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (6 Å)
Structure validation

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