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TitleMultiple molecular architectures of the eye lens chaperone αB-crystallin elucidated by a triple hybrid approach.
Journal, issue, pagesProc Natl Acad Sci U S A, Vol. 108, Issue 51, Page 20491-20496, Year 2011
Publish dateDec 20, 2011
AuthorsNathalie Braun / Martin Zacharias / Jirka Peschek / Andreas Kastenmüller / Juan Zou / Marianne Hanzlik / Martin Haslbeck / Juri Rappsilber / Johannes Buchner / Sevil Weinkauf /
PubMed AbstractThe molecular chaperone αB-crystallin, the major player in maintaining the transparency of the eye lens, prevents stress-damaged and aging lens proteins from aggregation. In nonlenticular cells, it ...The molecular chaperone αB-crystallin, the major player in maintaining the transparency of the eye lens, prevents stress-damaged and aging lens proteins from aggregation. In nonlenticular cells, it is involved in various neurological diseases, diabetes, and cancer. Given its structural plasticity and dynamics, structure analysis of αB-crystallin presented hitherto a formidable challenge. Here we present a pseudoatomic model of a 24-meric αB-crystallin assembly obtained by a triple hybrid approach combining data from cryoelectron microscopy, NMR spectroscopy, and structural modeling. The model, confirmed by cross-linking and mass spectrometry, shows that the subunits interact within the oligomer in different, defined conformations. We further present the molecular architectures of additional well-defined αB-crystallin assemblies with larger or smaller numbers of subunits, provide the mechanism how "heterogeneity" is achieved by a small set of defined structural variations, and analyze the factors modulating the oligomer equilibrium of αB-crystallin and thus its chaperone activity.
External linksProc Natl Acad Sci U S A / PubMed:22143763 / PubMed Central
MethodsEM (single particle)
Resolution9.4 Å
Structure data

1894

2ygd

EMDB-1894: Cryo-EM structure of alphaB-crystallin 24mer
PDB-2ygd: Molecular architectures of the 24meric eye lens chaperone alphaB- crystallin elucidated by a triple hybrid approach
Method: EM (single particle) / Resolution: 9.4 Å

Source
  • homo sapiens (human)
KeywordsCHAPERONE / PROTEIN AGGREGATION / HYBRID METHOD

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