The auto-orientation in high magnetic fields of oxidized cytochrome b562 as source of constraints for solution structure determination

@article{Arnesano2000TheAI,
  title={The auto-orientation in high magnetic fields of oxidized cytochrome b562 as source of constraints for solution structure determination},
  author={Fabio Arnesano and Lucia Banci and Ivano Bertini and Karin van der Wetering and Michael Czisch and R. Kaptein},
  journal={Journal of Biomolecular NMR},
  year={2000},
  volume={17},
  pages={295-304}
}
Abstract15N-1H 1J couplings were measured at 500 MHz and 800 MHz for 15N enriched oxidized cytochrome b562 from E. coli. The magnetic field dependence of 70 1J values, which could be measured without signal overlap, shows that there is a molecular magnetic anisotropy which provides partial molecular orientation in the magnetic field and, consequently, residual dipolar couplings (rdc). The rdc were used as further constraints to improve the existing structure [Arnesano et al. (1999) Biochemistry… 
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19 Citations

19 Citations

Citation Type

Citation Type

15N-1H Residual dipolar coupling analysis of native and alkaline-K79A Saccharomyces cerevisiae cytochrome c.
Backbone-only restraints for fast determination of the protein fold: the role of paramagnetism-based restraints. Cytochrome b562 as an example.
Solution structure calculations through self-orientation in a magnetic field of a cerium(III) substituted calcium-binding protein.
TLDR
It is shown that Ce(III), like low-spin Fe(III) in hemoproteins, is sufficiently magnetically anisotropic to induce self-orientation to an extent which can be exploited for solution structure determination.
NMR-validated structural model for oxidized Rhodopseudomonas palustris cytochrome c556
The structure of oxidized Rhodopseudomonas palustris cytochrome c556 has been modeled after that of high-spin cytochrome c′ from the same bacterium, the latter being the protein with the greatest…
Residual dipolar couplings in protein NMR
Partial molecular alignment leads to an incomplete averaging of anisotropic magnetic interactions such as the magnetic dipole–dipole interaction, the chemical shift anisotropy, or the electric…
Transient iron coordination sites in proteins: Exploiting the dual nature of paramagnetic NMR
Structure refinement of flexible proteins using dipolar couplings: Application to the protein p8MTCP1
TLDR
It is shown here that including DHNdip dipolar couplings in the structure calculation protocol improves the structure of the α-hairpin but not the positioning of the third helix, due to the motional averaging of the dip polar couplings measured in the last helix.
NMR study of the Escherichia coli 70S ribosome particle using residual dipolar couplings
TLDR
Together these data provide a solid foundation for an RDC methodology for application to the ribosome and RNCs, and will enable more detailed structural and dynamical studies of the emerging nascent chain.
An Italian contribution to structural genomics: Understanding metalloproteins
Structure-independent cross-validation between residual dipolar couplings originating from internal and external orienting media
TLDR
This structure-independent check shows the innocence of the orienting medium with respect to the structure of the protein in solution, and the simultaneous use of lanthanide substitution and external orienting media provides a further effective tool to control and tune the orientation tensor.
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References

The solution structure of paramagnetic metalloproteins.