Structural highlights
Function
[PFDA2_METJA] Molecular chaperone capable of stabilizing a range of proteins. Seems to fulfill an ATP-independent, HSP70-like function in archaeal de novo protein folding (By similarity).
Publication Abstract from PubMed
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.
Structural Determination of a Filamentous Chaperone to Fabricate Electronically Conductive Metalloprotein Nanowires.,Chen YX, Ing NL, Wang F, Xu D, Sloan NB, Lam NT, Winter DL, Egelman EH, Hochbaum AI, Clark DS, Glover DJ ACS Nano. 2020 May 7. doi: 10.1021/acsnano.9b09405. PMID:32347705[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Chen YX, Ing NL, Wang F, Xu D, Sloan NB, Lam NT, Winter DL, Egelman EH, Hochbaum AI, Clark DS, Glover DJ. Structural Determination of a Filamentous Chaperone to Fabricate Electronically Conductive Metalloprotein Nanowires. ACS Nano. 2020 May 7. doi: 10.1021/acsnano.9b09405. PMID:32347705 doi:http://dx.doi.org/10.1021/acsnano.9b09405
