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TitleThe structure and oxidation of the eye lens chaperone αA-crystallin.
Journal, issue, pagesNat Struct Mol Biol, Vol. 26, Issue 12, Page 1141-1150, Year 2019
Publish dateDec 2, 2019
AuthorsChristoph J O Kaiser / Carsten Peters / Philipp W N Schmid / Maria Stavropoulou / Juan Zou / Vinay Dahiya / Evgeny V Mymrikov / Beate Rockel / Sam Asami / Martin Haslbeck / Juri Rappsilber / Bernd Reif / Martin Zacharias / Johannes Buchner / Sevil Weinkauf /
PubMed AbstractThe 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 ...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.
External linksNat Struct Mol Biol / PubMed:31792453 / PubMed Central
MethodsEM (single particle)
Resolution9.0 - 9.8 Å
Structure data

4894

6t1r

EMDB-4894: Single particle cryo-EM reconstruction of a 16-mer assembly of reduced recombinant human alphaA-crystallin.
PDB-6t1r: Pseudo-atomic model of a 16-mer assembly of reduced recombinant human alphaA-crystallin (non domain swapped configuration)
Method: EM (single particle) / Resolution: 9.8 Å

EMDB-4895:
Single particle cryo-EM reconstruction of a 12-mer assembly of reduced recombinant human alphaA-crystallin.
Method: EM (single particle) / Resolution: 9.2 Å

EMDB-4896:
Single particle cryo-EM reconstruction of a 20-mer assembly of reduced recombinant human alphaA-crystallin.
Method: EM (single particle) / Resolution: 9.0 Å

Source
  • homo sapiens (human)
KeywordsCHAPERONE / sHsp / alphaA-crystallin / domain swapping

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