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 = {\#nosource, 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},
}
Downloads: 0
{"_id":"Rbe5WXt3AsAnEWt8j","bibbaseid":"jehle-rajagopal-bardiaux-markovic-khne-stout-higman-klevit-etal-solidstatenmrandsaxsstudiesprovideastructuralbasisfortheactivationofalphabcrystallinoligomers-2010","author_short":["Jehle, S.","Rajagopal, P.","Bardiaux, B.","Markovic, S.","Kühne, R.","Stout, J. R","Higman, V. A","Klevit, R. E","van Rossum, B.","Oschkinat, H."],"bibdata":{"bibtype":"article","type":"article","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":[{"propositions":[],"lastnames":["Jehle"],"firstnames":["Stefan"],"suffixes":[]},{"propositions":[],"lastnames":["Rajagopal"],"firstnames":["Ponni"],"suffixes":[]},{"propositions":[],"lastnames":["Bardiaux"],"firstnames":["Benjamin"],"suffixes":[]},{"propositions":[],"lastnames":["Markovic"],"firstnames":["Stefan"],"suffixes":[]},{"propositions":[],"lastnames":["Kühne"],"firstnames":["Ronald"],"suffixes":[]},{"propositions":[],"lastnames":["Stout"],"firstnames":["Joseph","R"],"suffixes":[]},{"propositions":[],"lastnames":["Higman"],"firstnames":["Victoria","A"],"suffixes":[]},{"propositions":[],"lastnames":["Klevit"],"firstnames":["Rachel","E"],"suffixes":[]},{"propositions":["van"],"lastnames":["Rossum"],"firstnames":["Barth-Jan"],"suffixes":[]},{"propositions":[],"lastnames":["Oschkinat"],"firstnames":["Hartmut"],"suffixes":[]}],"month":"September","year":"2010","pmid":"20802487","note":"Publisher: Nature Publishing Group, a division of Macmillan Publishers Limited. All Rights Reserved.","keywords":"#nosource, 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","bibtex":"@article{Jehle2010,\n\ttitle = {Solid-state {NMR} and {SAXS} studies provide a structural basis for the activation of {alphaB}-crystallin oligomers.},\n\tvolume = {17},\n\tissn = {1545-9985},\n\tshorttitle = {Nat {Struct} {Mol} {Biol}},\n\turl = {http://dx.doi.org/10.1038/nsmb.1891},\n\tdoi = {10.1038/nsmb.1891},\n\tabstract = {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.},\n\tnumber = {9},\n\tjournal = {Nature structural \\& molecular biology},\n\tauthor = {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},\n\tmonth = sep,\n\tyear = {2010},\n\tpmid = {20802487},\n\tnote = {Publisher: Nature Publishing Group, a division of Macmillan Publishers Limited. All Rights Reserved.},\n\tkeywords = {\\#nosource, 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},\n\tpages = {1037--1042},\n}\n\n\n\n","author_short":["Jehle, S.","Rajagopal, P.","Bardiaux, B.","Markovic, S.","Kühne, R.","Stout, J. R","Higman, V. A","Klevit, R. E","van Rossum, B.","Oschkinat, H."],"key":"Jehle2010","id":"Jehle2010","bibbaseid":"jehle-rajagopal-bardiaux-markovic-khne-stout-higman-klevit-etal-solidstatenmrandsaxsstudiesprovideastructuralbasisfortheactivationofalphabcrystallinoligomers-2010","role":"author","urls":{"Paper":"http://dx.doi.org/10.1038/nsmb.1891"},"keyword":["#nosource","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"],"metadata":{"authorlinks":{}},"html":""},"bibtype":"article","biburl":"https://bibbase.org/zotero/subhradip.paul","dataSources":["epdxi2MtNPwoQCL4d"],"keywords":["#nosource","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"],"search_terms":["solid","state","nmr","saxs","studies","provide","structural","basis","activation","alphab","crystallin","oligomers","jehle","rajagopal","bardiaux","markovic","kühne","stout","higman","klevit","van rossum","oschkinat"],"title":"Solid-state NMR and SAXS studies provide a structural basis for the activation of alphaB-crystallin oligomers.","year":2010}