2YGD

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


Experimental Data Snapshot

  • Method: ELECTRON MICROSCOPY
  • Resolution: 9.40 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 

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This is version 1.3 of the entry. See complete history


Literature

Multiple Molecular Architectures of the Eye Lens Chaperone Alpha Beta-Crystallin Elucidated by a Triple Hybrid Approach

Braun, N.Zacharias, M.Peschek, J.Kastenmueller, A.Zou, J.Hanzlik, M.Haslbeck, M.Rappsilber, J.Buchner, J.Weinkauf, S.

(2011) Proc Natl Acad Sci U S A 108: 20491

  • DOI: https://doi.org/10.1073/pnas.1111014108
  • Primary Citation of Related Structures:  
    2YGD

  • 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.


  • Organizational Affiliation

    Center for Integrated Protein Science Munich, Chemistry Department, Technische Universität München, Lichtenbergstrasse 4, 85747 Garching, Germany.


Macromolecules
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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
ALPHA-CRYSTALLIN B CHAIN
A, B, C, D, E
A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V, W, X
175Homo sapiensMutation(s): 0 
UniProt & NIH Common Fund Data Resources
Find proteins for P02511 (Homo sapiens)
Explore P02511 
Go to UniProtKB:  P02511
PHAROS:  P02511
GTEx:  ENSG00000109846 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP02511
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: ELECTRON MICROSCOPY
  • Resolution: 9.40 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 
EM Software:
TaskSoftware PackageVersion
RECONSTRUCTIONIMAGIC

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2011-12-07
    Type: Initial release
  • Version 1.1: 2012-01-11
    Changes: Other
  • Version 1.2: 2013-11-20
    Changes: Source and taxonomy
  • Version 1.3: 2018-10-03
    Changes: Data collection