A pH Switch for β‐Sheet Protein Folding

Anderson, Jordan M.; Andersen, Niels H.

doi:10.1002/ange.201700860

Cited by 2 publications

(3 citation statements)

References 28 publications

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“…The 15 N-labeled proteins for NMR titration experiments were expressed in M9 medium containing 15 N-labeled NH 4 Cl as the sole nitrogen source and purified by the same procedures for nonlabeled proteins. The NMR titration experiments were performed on a Bruker 600-MHz NMR spectrometer at 298 K with standard 1 H- 15 N HSQC pulse program.…”

Section: Nmr Titration Experimentsmentioning

confidence: 99%

“…The pH of a solution is important for the chemical reactions involved in life processes. pH-dependent conformational switches in proteins are involved in many biological processes, and pH-dependent biomolecules can also be developed as sensors and switches in biotechnology (1)(2)(3)(4). Most pH-dependent conformational changes in proteins result in an "on-off" switch, which is useful in protein design and the development of functional biomaterials (5,6).…”

Section: Introductionmentioning

confidence: 99%

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Discovery and mechanism of a pH-dependent dual-binding-site switch in the interaction of a pair of protein modules

et al. 2020

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Many important proteins undergo pH-dependent conformational changes resulting in “on-off” switches for protein function, which are essential for regulation of life processes and have wide application potential. Here, we report a pair of cellulosomal assembly modules, comprising a cohesin and a dockerin from Clostridium acetobutylicum, which interact together following a unique pH-dependent switch between two functional sites rather than on-off states. The two cohesin-binding sites on the dockerin are switched from one to the other at pH 4.8 and 7.5 with a 180° rotation of the bound dockerin. Combined analysis by nuclear magnetic resonance spectroscopy, crystal structure determination, mutagenesis, and isothermal titration calorimetry elucidates the chemical and structural mechanism of the pH-dependent switching of the binding sites. The pH-dependent dual-binding-site switch not only represents an elegant example of biological regulation but also provides a new approach for developing pH-dependent protein devices and biomaterials beyond an on-off switch for biotechnological applications.

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Section: Nmr Titration Experimentsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Discovery and mechanism of a pH-dependent dual-binding-site switch in the interaction of a pair of protein modules

et al. 2020

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“…This is because stability of the folded structures needs to be maintained by fewer interactions, and also active sites are to be designed within a small structural fold. However, miniaturized proteins are of substantial importance in therapeutics and biotechnology [6][7][8][9] .…”

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confidence: 99%

Expanding heme-protein folding space using designed multi-heme β-sheet mini-proteins

2018

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Nature has primarily exploited helical proteins, over β-sheets, for heme/multi-heme coordination. Understating of heme-protein structures has motivated the design of heme proteins utilizing coiled-coil helical structure. By contrast, de novo designed β-sheet proteins are less successful. However, designing proteins with discretely folded β-sheet structures encoding specific functions would have great potential for the development of new synthetic molecules e.g. enzymes, inhibitors. Here we report the design and characterization of multi-heme binding four-, six-, eight-, and twelve-stranded β-sheet mini-proteins (<40 amino acids) and proteins. Atomic-resolution structures demonstrate an expected β-sheet structural topology. The designed β-sheet mini-proteins pack or latch multiple hemes with high affnity in versatile orientations either by stacking or sideways, mimicking naturally occuring multi-heme protein conduits. The designed multi-stranded β-sheet heme proteins could serve as a platform for the generation of novel synthetic β-sheet protein mimics.

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A pH Switch for β‐Sheet Protein Folding

Cited by 2 publications

References 28 publications

Discovery and mechanism of a pH-dependent dual-binding-site switch in the interaction of a pair of protein modules

Discovery and mechanism of a pH-dependent dual-binding-site switch in the interaction of a pair of protein modules

Expanding heme-protein folding space using designed multi-heme β-sheet mini-proteins

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