Crystal Structure of the Calcium-Loaded Spherulin 3a Dimer Sheds Light on the Evolution Of the Eye Lens βγ-Crystallin Domain Fold

@article{Clout2001CrystalSO,
  title={Crystal Structure of the Calcium-Loaded Spherulin 3a Dimer Sheds Light on the Evolution Of the Eye Lens $\beta$$\gamma$-Crystallin Domain Fold},
  author={N. J. Clout and M. Kretschmar and R. Jaenicke and C. Slingsby},
  journal={Structure},
  year={2001},
  volume={9},
  pages={115-124}
}
Abstract Background: The βγ-crystallins belong to a superfamily of two-domain proteins found in vertebrate eye lenses, with distant relatives occurring in microorganisms. It has been considered that an eukaryotic stress protein, spherulin 3a, from the slime mold Physarum polycephalum shares a common one-domain ancestor with crystallins, similar to the one-domain 3-D structure determined by NMR. Results: The X-ray structure of spherulin 3a shows it to be a tight homodimer, which is consistent… Expand
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The structure of the homodimer of the N-terminal domain of rat betaB2- Crystallin resembles the ancestral prototype of the betagamma-crystallin superfamily as it self-associates in solution to form a dimer with an essentially identical domain interface as that between the N and C domains in betag AMs, but without the benefit of a covalent linker. Expand
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TLDR
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Myxococcus xanthus spore coat protein S, a stress-induced member of the βγ-crystallin superfamily, gains stability from binding of calcium ions
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