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

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 p...

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Published in	Biochimica et biophysica acta Vol. 1865; no. 11; pp. 1383 - 1394
Main Authors	Freedman, Robert B., Desmond, Jasmine L., Byrne, Lee J., Heal, Jack W., Howard, Mark J., Sanghera, Narinder, Walker, Kelly L., Wallis, A. Katrine, Wells, Stephen A., Williamson, Richard A., Römer, Rudolf A.
Format	Journal Article
Language	English
Published	Netherlands Elsevier B.V 01.11.2017 Elsevier Pub. Co
Subjects	Animals Biocatalysis Conserved Sequence Endoplasmic reticulum Endoplasmic Reticulum - enzymology Gene Expression Humans Molecular Chaperones - chemistry Molecular Chaperones - genetics Molecular Chaperones - metabolism Molecular Dynamics Simulation Oxidation-Reduction Oxidative protein folding Protein disulfide isomerase Protein Disulfide-Isomerases - chemistry Protein Disulfide-Isomerases - genetics Protein Disulfide-Isomerases - metabolism Protein Domains Protein dynamics Protein Folding Protein Structure, Secondary Saccharomyces cerevisiae - enzymology Saccharomyces cerevisiae - genetics Structural Homology, Protein Protein disulfide isomerase Protein dynamics Oxidative protein folding Endoplasmic reticulum
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Summary:	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.
Bibliography:	ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-3 content type line 23 ObjectType-Review-1 Current address: Cancer Research-UK Manchester Institute, Manchester M20 4BX, UK. Current address: School of Life Sciences, Coventry University, Coventry CV1 5FB, UK. Current address: Department of Chemical Engineering, University of Bath, Bath BA2 7AY, UK. Current address: School of Human and Life Sciences, Canterbury Christ Church University, Canterbury CT1 IQU, UK. Current address: School of Molecular Sciences and CMCA, University of Western Australia, Perth WA 6009, Australia. Current address: Immunocore Ltd., Milton Park, Abingdon OX14 4SA, UK. Current address: Warwick Medical School, Warwick University, CV4 7AL, UK. Alternative address: Department of Physics and Optoelectronics, Xiangtan University, Xiangtan 411105, Hunan, China. Current address: Department of Chemistry, University of Basel, CH-4056 Basel, Switzerland.
ISSN:	1570-9639 0006-3002 1878-1454 1878-2434
DOI:	10.1016/j.bbapap.2017.08.014