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Multiscale conformational heterogeneity in staphylococcal protein a: possible determinant of functional plasticity.

Publication ,  Journal Article
Deis, LN; Pemble, CW; Qi, Y; Hagarman, A; Richardson, DC; Richardson, JS; Oas, TG
Published in: Structure
October 7, 2014

The Staphylococcus aureus virulence factor staphylococcal protein A (SpA) is a major contributor to bacterial evasion of the host immune system, through high-affinity binding to host proteins such as antibodies. SpA includes five small three-helix-bundle domains (E-D-A-B-C) separated by conserved flexible linkers. Prior attempts to crystallize individual domains in the absence of a binding partner have apparently been unsuccessful. There have also been no previous structures of tandem domains. Here we report the high-resolution crystal structures of a single C domain, and of two B domains connected by the conserved linker. Both structures exhibit extensive multiscale conformational heterogeneity, which required novel modeling protocols. Comparison of domain structures shows that helix1 orientation is especially heterogeneous, coordinated with changes in side chain conformational networks and contacting protein interfaces. This represents the kind of structural plasticity that could enable SpA to bind multiple partners.

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Published In

Structure

DOI

EISSN

1878-4186

Publication Date

October 7, 2014

Volume

22

Issue

10

Start / End Page

1467 / 1477

Location

United States

Related Subject Headings

  • Staphylococcus aureus
  • Staphylococcal Protein A
  • Protein Structure, Tertiary
  • Protein Conformation
  • Models, Molecular
  • Crystallography, X-Ray
  • Biophysics
  • 34 Chemical sciences
  • 31 Biological sciences
  • 08 Information and Computing Sciences
 

Citation

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Deis, L. N., Pemble, C. W., Qi, Y., Hagarman, A., Richardson, D. C., Richardson, J. S., & Oas, T. G. (2014). Multiscale conformational heterogeneity in staphylococcal protein a: possible determinant of functional plasticity. Structure, 22(10), 1467–1477. https://doi.org/10.1016/j.str.2014.08.014
Deis, Lindsay N., Charles W. Pemble, Yang Qi, Andrew Hagarman, David C. Richardson, Jane S. Richardson, and Terrence G. Oas. “Multiscale conformational heterogeneity in staphylococcal protein a: possible determinant of functional plasticity.Structure 22, no. 10 (October 7, 2014): 1467–77. https://doi.org/10.1016/j.str.2014.08.014.
Deis LN, Pemble CW, Qi Y, Hagarman A, Richardson DC, Richardson JS, et al. Multiscale conformational heterogeneity in staphylococcal protein a: possible determinant of functional plasticity. Structure. 2014 Oct 7;22(10):1467–77.
Deis, Lindsay N., et al. “Multiscale conformational heterogeneity in staphylococcal protein a: possible determinant of functional plasticity.Structure, vol. 22, no. 10, Oct. 2014, pp. 1467–77. Pubmed, doi:10.1016/j.str.2014.08.014.
Deis LN, Pemble CW, Qi Y, Hagarman A, Richardson DC, Richardson JS, Oas TG. Multiscale conformational heterogeneity in staphylococcal protein a: possible determinant of functional plasticity. Structure. 2014 Oct 7;22(10):1467–1477.
Journal cover image

Published In

Structure

DOI

EISSN

1878-4186

Publication Date

October 7, 2014

Volume

22

Issue

10

Start / End Page

1467 / 1477

Location

United States

Related Subject Headings

  • Staphylococcus aureus
  • Staphylococcal Protein A
  • Protein Structure, Tertiary
  • Protein Conformation
  • Models, Molecular
  • Crystallography, X-Ray
  • Biophysics
  • 34 Chemical sciences
  • 31 Biological sciences
  • 08 Information and Computing Sciences