2KLR
Solid-state NMR structure of the alpha-crystallin domain in alphaB-crystallin oligomers
Summary for 2KLR
| Entry DOI | 10.2210/pdb2klr/pdb |
| Descriptor | Alpha-crystallin B chain (1 entity in total) |
| Functional Keywords | protein, dimer, oligomer, heterogeneity, intermolecular interactions, chaperone, shsp, human, small heat-shock protein, cataract, desmin-related myopathy, disease mutation, eye lens protein, glycoprotein, methylation, oxidation, phosphoprotein |
| Biological source | Homo sapiens (human) |
| Cellular location | Cytoplasm: P02511 |
| Total number of polymer chains | 2 |
| Total formula weight | 40383.86 |
| Authors | Jehle, S.,Rajagopal, P.,Markovic, S.,Bardiaux, B.,Kuehne, R.,Higman, V.A.,Klevit, R.E.,van Rossum, B.,Oschkinat, H. (deposition date: 2009-07-08, release date: 2010-07-07, Last modification date: 2024-05-01) |
| Primary citation | Jehle, S.,Rajagopal, P.,Bardiaux, B.,Markovic, S.,Kuhne, R.,Stout, J.R.,Higman, V.A.,Klevit, R.E.,van Rossum, B.J.,Oschkinat, H. Solid-state NMR and SAXS studies provide a structural basis for the activation of alphaB-crystallin oligomers. Nat.Struct.Mol.Biol., 17:1037-1042, 2010 Cited by PubMed 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. PubMed: 20802487DOI: 10.1038/nsmb.1891 PDB entries with the same primary citation |
| Experimental method | SOLID-STATE NMR |
Structure validation
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