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

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. ISSN 0006-3002.

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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.

Item Type: Article
Subjects: Q Science > QD Chemistry > QD0241 Organic chemistry > QD0415 Biochemistry
Divisions: Faculty of Social and Applied Sciences > School of Human and Life Sciences
Depositing User: Dr Lee Byrne
Date Deposited: 30 Aug 2017 09:59
Last Modified: 31 Oct 2017 16:22
URI: https://create.canterbury.ac.uk/id/eprint/16260

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Last edited: 29/06/2016 12:23:00