Rosinke, Burkhard and Renner, Christian and Mayr, Eva-Maria and Jaenicke, Rainer and Holak, Tad A. (1997) Ca2+-loaded spherulin 3a from Physarum polycephalum adopts the prototype gamma-crystallin fold in aqueous solution. JOURNAL OF MOLECULAR BIOLOGY, 271 (4). pp. 645-655. ISSN 0022-2836, 1089-8638
Full text not available from this repository.Abstract
Spherulin 3a is the most abundantly expressed cytosolic protein in spherulating plasmodia of the slime mold Physarum polycephalum. High yields of unlabeled, uniformly N-15 and uniformly C-13/N-15-labeled recombinant spherulin 3a from Escherichia coli could be produced by a simple protocol described here. The three-dimensional solution structure of Ca2+-loaded spherulin 3a was determined by home-and heteronuclear NMR spec troscopy. The structure of monomeric spherulin 3a consists of two pleated beta-sheets plus a short alpha-helix arranged into the gamma-crystallin fold. The beta-sheets comprise two intertwined Greek-key motifs. An additional N-terminal beta-strand is unique to spherulin 3a. Complexation of calcium ions greatly enhances overall conformational stability of the protein. The average atomic root-mean-square deviations (r.m.s.d.) for heavy atoms in beta-strands were 0.34(+/-0.16) Angstrom for the backbone atoms and 0.73(+/-0.40) Angstrom for all atoms. The corresponding r.m.s.d. values for heavy atoms in the whole protein were 0.62(+/-0.42) Angstrom for the backbone atoms and 0.99(+/-0.65) A for all atoms. We show the structural relationship between spherulin 3a, a myxomycete dormancy protein, and crystallins from the vertebrate eye lens. Since spherulin 3a has a structure corresponding to one domain of bovine gamma B(II)-crystallin, it represents a hypothetical ancestral gamma-crystallin precursor structure. (C) 1997 Academic Press Limited.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | NUCLEAR-MAGNETIC-RESONANCE; NOESY-HSQC EXPERIMENT; LENS CRYSTALLINS; LARGER PROTEINS; EYE LENS; NMR; SPECTROSCOPY; EVOLUTION; SPECTRA; SUPPRESSION; NMR; spherulin structure; Physarum polycephalum; beta gamma-crystallin superfamily; protein evolution |
| Subjects: | 500 Science > 540 Chemistry & allied sciences 500 Science > 570 Life sciences |
| Divisions: | Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 30 Mar 2023 08:10 |
| Last Modified: | 30 Mar 2023 08:10 |
| URI: | https://pred.uni-regensburg.de/id/eprint/50638 |
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