6T1R
Pseudo-atomic model of a 16-mer assembly of reduced recombinant human alphaA-crystallin (non domain swapped configuration)
Summary for 6T1R
| Entry DOI | 10.2210/pdb6t1r/pdb |
| EMDB information | 4894 |
| Descriptor | Alpha-crystallin A chain (1 entity in total) |
| Functional Keywords | shsp, alphaa-crystallin, domain swapping, chaperone |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 16 |
| Total formula weight | 318981.02 |
| Authors | Peters, C.,Kaiser, C.J.O.,Weinkauf, S.,Zacharias, M.,Buchner, J. (deposition date: 2019-10-05, release date: 2019-12-11, Last modification date: 2024-05-15) |
| Primary citation | Kaiser, C.J.O.,Peters, C.,Schmid, P.W.N.,Stavropoulou, M.,Zou, J.,Dahiya, V.,Mymrikov, E.V.,Rockel, B.,Asami, S.,Haslbeck, M.,Rappsilber, J.,Reif, B.,Zacharias, M.,Buchner, J.,Weinkauf, S. The structure and oxidation of the eye lens chaperone alpha A-crystallin. Nat.Struct.Mol.Biol., 26:1141-1150, 2019 Cited by PubMed Abstract: The small heat shock protein αA-crystallin is a molecular chaperone important for the optical properties of the vertebrate eye lens. It forms heterogeneous oligomeric ensembles. We determined the structures of human αA-crystallin oligomers by combining cryo-electron microscopy, cross-linking/mass spectrometry, NMR spectroscopy and molecular modeling. The different oligomers can be interconverted by the addition or subtraction of tetramers, leading to mainly 12-, 16- and 20-meric assemblies in which interactions between N-terminal regions are important. Cross-dimer domain-swapping of the C-terminal region is a determinant of αA-crystallin heterogeneity. Human αA-crystallin contains two cysteines, which can form an intramolecular disulfide in vivo. Oxidation in vitro requires conformational changes and oligomer dissociation. The oxidized oligomers, which are larger than reduced αA-crystallin and destabilized against unfolding, are active chaperones and can transfer the disulfide to destabilized substrate proteins. The insight into the structure and function of αA-crystallin provides a basis for understanding its role in the eye lens. PubMed: 31792453DOI: 10.1038/s41594-019-0332-9 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (9.8 Å) |
Structure validation
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