Purification, crystallization and X-ray structures of the two manganese superoxide dismutases from Caenorhabditis elegans
2008

Study of Manganese Superoxide Dismutases from C. elegans

publication Evidence: high

Author Information

Author(s): Trinh Chi H., Hunter Thérèse, Stewart Emma E., Phillips Simon E. V., Hunter Gary J.

Primary Institution: University of Leeds

Hypothesis

The study investigates the structural characteristics of two manganese superoxide dismutases from Caenorhabditis elegans.

Conclusion

The structures of the two manganese superoxide dismutases from C. elegans are very similar to the human manganese superoxide dismutase.

Supporting Evidence

  • The structures of MnSOD-2 and MnSOD-3 were determined to 1.8 and 1.7 Å resolution, respectively.
  • Both proteins were found to be tetrameric in structure.
  • The final structure of MnSOD-3 was refined to R = 21.6% and R_free = 26.2% at 293 K.
  • The structures revealed a striking similarity to human manganese superoxide dismutase.

Takeaway

Scientists looked at two proteins from a tiny worm that help protect cells from damage, and found they are very similar to a protein in humans.

Methodology

The proteins were expressed in E. coli, purified using metal-chelation affinity chromatography, and their structures were determined using X-ray crystallography.

Digital Object Identifier (DOI)

10.1107/S1744309108037056

Want to read the original?

Access the complete publication on the publisher's website

View Original Publication