2YGD

Molecular architectures of the 24meric eye lens chaperone alphaB- crystallin elucidated by a triple hybrid approach

Summary for 2YGD

• Entry DOI: 10.2210/pdb2ygd/pdb
• Related: 2KLR 2WJ7 2Y1Y 2Y1Z 2Y22
• EMDB information: 1894
• Descriptor: ALPHA-CRYSTALLIN B CHAIN (1 entity in total)
• Functional Keywords: chaperone, protein aggregation, hybrid method
• Biological source: HOMO SAPIENS (HUMAN)
• Total number of polymer chains: 24
• Total formula weight: 484606.32

Authors

Braun, N.,Zacharias, M.,Peschek, J.,Kastenmueller, A.,Zou, J.,Hanzlik, M.,Haslbeck, M.,Rappsilber, J.,Buchner, J.,Weinkauf, S. (deposition date: 2011-04-13, release date: 2011-12-07, Last modification date: 2024-05-08)

Primary citation

Braun, N.,Zacharias, M.,Peschek, J.,Kastenmueller, A.,Zou, J.,Hanzlik, M.,Haslbeck, M.,Rappsilber, J.,Buchner, J.,Weinkauf, S.
Multiple Molecular Architectures of the Eye Lens Chaperone Alpha Beta-Crystallin Elucidated by a Triple Hybrid Approach
Proc.Natl.Acad.Sci.USA, 108:20491-, 2011

PubMed Abstract: 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.

PubMed: 22143763
DOI: 10.1073/PNAS.1111014108

Experimental method

ELECTRON MICROSCOPY (9.4 Å)