‘Something in the way she moves’: The functional significance of flexibility in the multiple roles of protein disulfide isomerase (PDI)

Journal article


Freedman, R., Desmond, J., Byrne, L., Heal, J., Howard, M., Sanghera, N., Walker, K., Wallis, A., Wells, S., Williamson, R. and Romer, R. 2017. ‘Something in the way she moves’: The functional significance of flexibility in the multiple roles of protein disulfide isomerase (PDI). Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1865 (11 (A)), pp. 1383-1394.
AuthorsFreedman, R., Desmond, J., Byrne, L., Heal, J., Howard, M., Sanghera, N., Walker, K., Wallis, A., Wells, S., Williamson, R. and Romer, R.
Abstract

Protein disulfide isomerase (PDI) has diverse functions in the endoplasmic reticulum as catalyst of redox transfer, disulfide isomerization and oxidative protein folding, as molecular chaperone and in multi-subunit complexes. It interacts with an extraordinarily wide range of substrate and partner proteins, but there is only limited structural information on these interactions. Extensive evidence on the flexibility of PDI in solution is not matched by any detailed picture of the scope of its motion.

A new rapid method for simulating the motion of large proteins provides detailed molecular trajectories for PDI demonstrating extensive changes in the relative orientation of its four domains, great variation in the distances between key sites and internal motion within the core ligand-binding domain. The review shows that these simulations are consistent with experimental evidence and provide insight into the functional capabilities conferred by the extensive flexible motion of PDI.

Year2017
JournalBiochimica et Biophysica Acta (BBA) - Proteins and Proteomics
Journal citation1865 (11 (A)), pp. 1383-1394
PublisherElsevier
ISSN0006-3002
Digital Object Identifier (DOI)doi:10.1016/j.bbapap.2017.08.014
FunderBBSRC (BB/DO1 787)
Wellcome Trust (093125/z/10Z)
EPSRC
Publication dates
Online24 Aug 2017
Publication process dates
Deposited30 Aug 2017
Accepted10 Aug 2017
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Chaudhary, S., Khokhar, W., Jabre, I., Reddy A.S.N., Byrne, L., Wilson, C.M. and Syed, N. 2019. Alternative splicing and protein diversity: plants versus animals. Frontiers in Plant Science. 10 (708).
Winter Aconite (Eranthis hyemalis) Lectin as a cytotoxic effector in the lifecycle of Caenorhabditis elegans
McConnell, M., Lisgarten, D., Byrne, L., Harvey, S. and Bertolo-Pardo, E. 2015. Winter Aconite (Eranthis hyemalis) Lectin as a cytotoxic effector in the lifecycle of Caenorhabditis elegans. PeerJ.
Cell division is essential for elimination of the yeast [PSI+] prion by guanidine hydrochloride
Byrne, L., Cox, B., Coleman, D., Ridout, M., Morgan, B. and Tuiteq, M. 2007. Cell division is essential for elimination of the yeast [PSI+] prion by guanidine hydrochloride. Proceedings of the National Academy of Sciences of the United States of America (PNAS). 104 (28), pp. 11688-11693.
The number and transmission of [PSI+] prion seeds (Propagons) in the yeast Saccharomyces cerevisiae
Byrne, L., Cole, D., Cox, B., Ridout, M., Morgan, B. and Tuite, M. 2009. The number and transmission of [PSI+] prion seeds (Propagons) in the yeast Saccharomyces cerevisiae. PLoS ONE. 4 (3), p. e4670.
Mapping of the ligand-binding site on the b′ domain of human PDI: interaction with peptide ligands and the x-linker region
Byrne, L., Sidhu, A., Wallis, A., Ruddock, L., Freedman, R., Howard, M. and Williamson, R. 2009. Mapping of the ligand-binding site on the b′ domain of human PDI: interaction with peptide ligands and the x-linker region. Biochemical Journal. 423 (2), pp. 209-217.
The ligand-binding b' domain of human protein disulphide-isomerase mediates homodimerization
Wallis, A., Sidhu, A., Byrne, L., Howard, M., Ruddock, L., Williamson, R. and Freedman, R. 2009. The ligand-binding b' domain of human protein disulphide-isomerase mediates homodimerization. Protein Science. 18 (12), pp. 2569-2577.