Ca2+-loaded spherulin 3a from Physarum polycephalum adopts the prototype gamma-crystallin fold in aqueous solution.
作者： Burkhard Rosinke , Christian Renner , Eva-Maria Mayr , Rainer Jaenicke , Tad A Holak
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摘要: Abstract Spherulin 3a is the most abundantly expressed cytosolic protein in spherulating plasmodia of slime mold Physarum polycephalum. High yields unlabeled, uniformly 15N and 13C/15N-labeled recombinant spherulin from Escherichia coli could be produced by a simple protocol described here. The three-dimensional solution structure Ca2+-loaded was determined homo- heteronuclear NMR spectroscopy. monomeric consists two pleated β-sheets plus short α-helix arranged into γ-crystallin fold. comprise intertwined Greek-key motifs. An additional N-terminal β-strand unique to 3a. Complexation calcium ions greatly enhances overall conformational stability protein. average atomic root-mean-square deviations (r.m.s.d.) for heavy atoms β-strands were 0.34(±0.16) A backbone 0.73(±0.40) all atoms. corresponding r.m.s.d. values whole 0.62(±0.42) 0.99(±0.65) We show structural relationship between 3a, myxomycete dormancy protein, crystallins vertebrate eye lens. Since has one domain bovine γB(II)-crystallin, it represents hypothetical ancestral precursor structure.
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