Dresden 2014 – wissenschaftliches Programm
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BP: Fachverband Biologische Physik
BP 14: Posters: Protein Structure and dynamics
BP 14.9: Poster
Dienstag, 1. April 2014, 09:30–12:30, P1
Dynamics of the family of protein disulfide isomerases. — •Jack Heal1, Stephen Well2, Emilio Jimenez-Roldan1, Rudolf Römer1, and Robert Freedman1 — 1University of Warwick, Coventry, England, CV4 7AL — 2University of Bath, Bath, England, BA2 7AY
Protein disulfide isomerase (PDI) is a multifunctional enzyme that facilitates protein folding by disulfide bond formation and isomerisation. PDI consists of four thioredoxin-fold domains; the other members of the PDI family are formed of a small number of homologous domains. The function of some of the members is not well understood or characterised. Recently, the structure of human PDI has been determined for the first time through X-ray crystallography. These data add to a small number of previous X-ray crystal structures of the PDI family members that are available in the protein data bank. With these structures as input, we use rapid computational methods to simulate their overall flexibility and dynamics. We study quantitatively the relative domain orientations as well as the distance between functional sites, extending our recent study on yeast PDI. From this information, we construct a map of these motions and discuss the protein dynamics of the PDI family in the context of structure, sequence and function. We aim to use these techniques along with the experimental data available to fully characterise the whole family and use structure-derived information to inform discussion of protein function in general.