Alice E. Parnell
University of Southampton
5 Papers
Alice E. Parnell is an academic researcher from University of Southampton. The author has contributed to research in topics: Polyphosphate & Polyphosphate kinase. The author has an hindex of 2, co-authored 2 publications.
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Papers
An expandable, modular de novo protein platform for precision redox engineering
George H. Hutchins,Claire E.M. Noble,H. Adrian Bunzel,Christopher B. Williams,P. Dubiel,Sathish K. N. Yadav,Paul M. Molinaro,R. Barringer,Hector Blackburn,Benjamin J. Hardy,Alice E. Parnell,Charles Landau,Paul R. Race,Thomas A. Oliver,Ronald L. Koder,Matthew P. Crump,Christiane Schaffitzel,A. Sofia F. Oliveira,Adrian J. Mulholland,J. L. Ross Anderson +19 more
TL;DR: The design of an expandable, modular protein platform for creating well-folded, new-to-nature proteins containing one or more redox-active heme cofactors is reported and it is demonstrated that a relatively simple computational design strategy can be used to extend heme-containing modules into a 7-nm molecular wire.
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The Role of Cytochrome P450 AbyV in the Final Stages of Abyssomicin C Biosynthesis
Andrew Devine,Alice E. Parnell,Catherine R. Back,Nicholas R. Lees,Samuel T Johns,Ainul Zura Zulkepli,R. Barringer,Katja Zorn,James E. M. Stach,Matthew P. Crump,Martin A. Hayes,Marc W. van der Kamp,Paul R. Race,Christine L. Willis +13 more
TL;DR: In this paper , the X-ray crystal structure of AbyV has been determined, which in combination with molecular dynamics simulations provides a structural framework for their functional data, and demonstrates the power of combining selective carbon-13 labeling with NMR spectroscopy as a sensitive tool to interrogate enzyme-catalysed reactions in vitro with no need for purification.
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Domain shuffling of a highly mutable ligand‐binding fold drives adhesin generation across the bacterial kingdom
R. Barringer,Alice E. Parnell,Aleix Lafita,Vivian A. Monzon,Catherine R. Back,Mariusz Madej,Jan Potempa,Angela H. Nobbs,Steven G. Burston,Alex Bateman,Paul R. Race +10 more
TL;DR: In this paper, the early stages of structural and functional divergence in Csh proteins were investigated by determining the X-ray crystal structure of the CshB adhesive domain NR2 and characterizing its Fn•binding properties in vitro.
1
Substrate recognition and mechanism revealed by ligand-bound polyphosphate kinase 2 structures.
Alice E. Parnell,Silja Mordhorst,Florian Kemper,Mariacarmela Giurrandino,Josh P. Prince,Nikola J. Schwarzer,Alexandre Hofer,Daniel Wohlwend,Henning J. Jessen,Henning J. Jessen,Stefan Gerhardt,Oliver Einsle,Petra C. F. Oyston,Petra C. F. Oyston,Jennifer N. Andexer,Peter L. Roach +15 more
TL;DR: The structural analysis and comparison of a class I PPK2 (ADP-phosphorylating) and a class III PPK 2 (AMP- and ADP-PhosphoryLating), both complexed with polyphosphate and/or nucleotide substrates are reported, which define the molecular basis of nucleotide specificity and are consistent with a Mg2+ catalyzed in-line phosphoryl transfer mechanism.
Biochemical and structural characterization of polyphosphate kinase 2 from the intracellular pathogen Francisella tularensis
TL;DR: The polyphosphate kinase 2 from the intracellular pathogen Francisella tularensis has been characterized by a range of biochemical methods and X-ray crystallography and the antibiotic sensitivity of a deletion mutant lacking the gene encoding PPK2 is reported.