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      19F NMR spectroscopy monitors ligand binding to recombinantly fluorine-labelled b′ x from human protein disulphide isomerase (hPDI)†

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          Abstract

          Fluoroindole recombinant protein labelling enables a 19F NMR study to observe protein–ligand binding and dissociation constant determination.

          Abstract

          We report a protein-observe 19F NMR-based ligand titration binding study of human PDI b′x with Δ-somatostatin that also emphasises the need to optimise recombinant protein fluorination when using 5- or 6-fluoroindole. This study highlights a recombinant preference for 5-fluoroindole over 6-fluoroindole; most likely due to the influence of fluorine atomic packing within the folded protein structure. Fluorination affords a single 19F resonance probe to follow displacement of the protein x-linker as ligand is titrated and provides a dissociation constant of 23 ± 4 μM.

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          Protein disulfide isomerase: a critical evaluation of its function in disulfide bond formation.

          Feras Hatahet, Lloyd W. Ruddock (2009)
          Disulfide bond formation is probably involved in the biogenesis of approximately one third of human proteins. A central player in this essential process is protein disulfide isomerase or PDI. PDI was the first protein-folding catalyst reported. However, despite more than four decades of study, we still do not understand much about its physiological mechanisms of action. This review examines the published literature with a critical eye. This review aims to (a) provide background on the chemistry of disulfide bond formation and rearrangement, including the concept of reduction potential, before examining the structure of PDI; (b) detail the thiol-disulfide exchange reactions that are catalyzed by PDI in vitro, including a critical examination of the assays used to determine them; (c) examine oxidation and reduction of PDI in vivo, including not only the role of ERo1 but also an extensive assessment of the role of glutathione, as well as other systems, such as peroxide, dehydroascorbate, and a discussion of vitamin K-based systems; (d) consider the in vivo reactions of PDI and the determination and implications of the redox state of PDI in vivo; and (e) discuss other human and yeast PDI-family members.
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            BIOCHEMISTRY

            R Krall, E. Plowman-Prine (1965)
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              The crystal structure of yeast protein disulfide isomerase suggests cooperativity between its active sites.

              William Lennarz, R Noiva, Hermann Schindelin … (2006)
              Protein disulfide isomerase plays a key role in catalyzing the folding of secretory proteins. It features two catalytically inactive thioredoxin domains inserted between two catalytically active thioredoxin domains and an acidic C-terminal tail. The crystal structure of yeast PDI reveals that the four thioredoxin domains are arranged in the shape of a twisted "U" with the active sites facing each other across the long sides of the "U." The inside surface of the "U" is enriched in hydrophobic residues, thereby facilitating interactions with misfolded proteins. The domain arrangement, active site location, and surface features strikingly resemble the Escherichia coli DsbC and DsbG protein disulfide isomerases. Biochemical studies demonstrate that all domains of PDI, including the C-terminal tail, are required for full catalytic activity. The structure defines a framework for rationalizing the differences between the two active sites and their respective roles in catalyzing the formation and rearrangement of disulfide bonds.
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                Author and article information

                Journal
                Journal ID (nlm-ta): Org Biomol Chem
                Journal ID (iso-abbrev): Org. Biomol. Chem
                Title: Organic & Biomolecular Chemistry
                Publisher: Royal Society of Chemistry
                ISSN (Print): 1477-0520
                ISSN (Electronic): 1477-0539
                Publication date (Print): 21 June 2014
                Publication date (Electronic): 6 May 2014
                Volume: 12
                Issue: 23
                Pages: 3808-3812
                Affiliations
                [a ] Protein Science Group , School of Biosciences , University of Kent , Giles Lane , Canterbury , Kent CT2 7NJ , UK . Email: r.a.williamson@ 123456kent.ac.uk ; Email: m.j.howard@ 123456kent.ac.uk
                Article
                Publisher ID: c4ob00699b
                DOI: 10.1039/c4ob00699b
                PMC ID: 4157668
                PubMed ID: 24796794
                SO-VID: c04df8d0-d28e-4770-a438-578ff47c98dc
                Copyright © This journal is © The Royal Society of Chemistry 2014
                License:

                This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License ( http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

                History
                Date received : 2 April 2014
                Date accepted : 29 April 2014
                Categories
                Subject: Chemistry

                Notes

                †Electronic supplementary information (ESI) available. See DOI: 10.1039/c4ob00699b


                ScienceOpen disciplines: Organic & Biomolecular chemistry
                Data availability:
                ScienceOpen disciplines: Organic & Biomolecular chemistry

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