Skip to main content

High-resolution NMR studies of structure and dynamics of human ERp27 indicate extensive interdomain flexibility

Amin, Nader T., Wallis, Anne Katrine, Wells, Stephen A., Rowe, Michelle L., Williamson, Richard A., Howard, Mark J., Freedman, Robert B. (2013) High-resolution NMR studies of structure and dynamics of human ERp27 indicate extensive interdomain flexibility. Biochemical Journal, 450 (2). pp. 321-332. ISSN 0264-6021. (doi:10.1042/BJ20121635) (The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided)

The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided. (Contact us about this Publication)
Official URL
http://dx.doi.org/10.1042/BJ20121635

Abstract

ERp27 (endoplasmic reticulum protein 27.7 kDa) is a homologue of PDI (protein disulfide-isomerase) localized to the endoplasmic reticulum. ERp27 is predicted to consist of two thioredoxin-fold domains homologous with the non-catalytic b and b' domains of PDI. The structure in solution of the N-terminal b-like domain of ERp27 was solved using high-resolution NMR data. The structure confirms that it has the thioredoxin fold and that ERp27 is a member of the PDI family. N-15-NMR relaxation data were obtained and ModelFree analysis highlighted limited exchange contributions and slow internal motions, and indicated that the domain has an average order parameter S' of 0.79. Comparison of the single-domain structure determined in the present study with the equivalent domain within full-length ERp27, determined independently by X-ray diffraction, indicated very close agreement. The domain interface inferred from NMR data in solution was much more extensive than that observed in the X-ray structure, suggesting that the domains flex independently and that crystallization selects one specific interdomain orientation. This led us to apply a new rapid method to simulate the flexibility of the full-length protein, establishing that the domains show considerable freedom to flex (tilt and twist) about the interdomain linker, consistent with the NMR data.

Item Type: Article
DOI/Identification number: 10.1042/BJ20121635
Uncontrolled keywords: ERp27, NMR, Structure determination, dynamics
Subjects: Q Science
Divisions: Faculties > Sciences > School of Biosciences
Depositing User: Richard Williamson
Date Deposited: 12 Jun 2013 15:40 UTC
Last Modified: 29 May 2019 10:17 UTC
Resource URI: https://kar.kent.ac.uk/id/eprint/34282 (The current URI for this page, for reference purposes)
  • Depositors only (login required):