Solid-state NMR and SAXS studies provide a structural basis for the activation of alphaB-crystallin oligomers. Jehle, S., Rajagopal, P., Bardiaux, B., Markovic, S., Kühne, R., Stout, J. R, Higman, V. A, Klevit, R. E, van Rossum, B., & Oschkinat, H. Nature structural & molecular biology, 17(9):1037–1042, September, 2010. Publisher: Nature Publishing Group, a division of Macmillan Publishers Limited. All Rights Reserved.![Solid-state NMR and SAXS studies provide a structural basis for the activation of alphaB-crystallin oligomers. [link]](https://bibbase.org/img/filetypes/link.svg "link")
Paper doi abstract bibtex The small heat shock protein alphaB-crystallin (alphaB) contributes to cellular protection against stress. For decades, high-resolution structural studies on oligomeric alphaB have been confounded by its polydisperse nature. Here, we present a structural basis of oligomer assembly and activation of the chaperone using solid-state NMR and small-angle X-ray scattering (SAXS). The basic building block is a curved dimer, with an angle of approximately 121 degrees between the planes of the beta-sandwich formed by alpha-crystallin domains. The highly conserved IXI motif covers a substrate binding site at pH 7.5. We observe a pH-dependent modulation of the interaction of the IXI motif with beta4 and beta8, consistent with a pH-dependent regulation of the chaperone function. N-terminal region residues Ser59-Trp60-Phe61 are involved in intermolecular interaction with beta3. Intermolecular restraints from NMR and volumetric restraints from SAXS were combined to calculate a model of a 24-subunit alphaB oligomer with tetrahedral symmetry.
@article{Jehle2010,
title = {Solid-state {NMR} and {SAXS} studies provide a structural basis for the activation of {alphaB}-crystallin oligomers.},
volume = {17},
issn = {1545-9985},
shorttitle = {Nat {Struct} {Mol} {Biol}},
url = {http://dx.doi.org/10.1038/nsmb.1891},
doi = {10.1038/nsmb.1891},
abstract = {The small heat shock protein alphaB-crystallin (alphaB) contributes to cellular protection against stress. For decades, high-resolution structural studies on oligomeric alphaB have been confounded by its polydisperse nature. Here, we present a structural basis of oligomer assembly and activation of the chaperone using solid-state NMR and small-angle X-ray scattering (SAXS). The basic building block is a curved dimer, with an angle of approximately 121 degrees between the planes of the beta-sandwich formed by alpha-crystallin domains. The highly conserved IXI motif covers a substrate binding site at pH 7.5. We observe a pH-dependent modulation of the interaction of the IXI motif with beta4 and beta8, consistent with a pH-dependent regulation of the chaperone function. N-terminal region residues Ser59-Trp60-Phe61 are involved in intermolecular interaction with beta3. Intermolecular restraints from NMR and volumetric restraints from SAXS were combined to calculate a model of a 24-subunit alphaB oligomer with tetrahedral symmetry.},
number = {9},
journal = {Nature structural \& molecular biology},
author = {Jehle, Stefan and Rajagopal, Ponni and Bardiaux, Benjamin and Markovic, Stefan and Kühne, Ronald and Stout, Joseph R and Higman, Victoria A and Klevit, Rachel E and van Rossum, Barth-Jan and Oschkinat, Hartmut},
month = sep,
year = {2010},
pmid = {20802487},
note = {Publisher: Nature Publishing Group, a division of Macmillan Publishers Limited. All Rights Reserved.},
keywords = {Analytical, Binding Sites, Biomolecular, Chemistry Techniques, Humans, Hydrogen-Ion Concentration, Models, Molecular, Nuclear Magnetic Resonance, Protein Structure, Quaternary, alpha-Crystallin B Chain, alpha-Crystallin B Chain: chemistry},
pages = {1037--1042},
}
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Here, we present a structural basis of oligomer assembly and activation of the chaperone using solid-state NMR and small-angle X-ray scattering (SAXS). The basic building block is a curved dimer, with an angle of approximately 121 degrees between the planes of the beta-sandwich formed by alpha-crystallin domains. The highly conserved IXI motif covers a substrate binding site at pH 7.5. We observe a pH-dependent modulation of the interaction of the IXI motif with beta4 and beta8, consistent with a pH-dependent regulation of the chaperone function. N-terminal region residues Ser59-Trp60-Phe61 are involved in intermolecular interaction with beta3. 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