3J07

Model of a 24mer alphaB-crystallin multimer


Experimental Data Snapshot

  • Method: SOLID-STATE NMR
  • Conformers Calculated: 200 
  • Conformers Submitted: 
  • Selection Criteria: structures with the lowest energy 

  • Method: SOLUTION SCATTERING

  • Method: ELECTRON MICROSCOPY
  • Resolution: 20.0 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 

wwPDB Validation   3D Report Full Report

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This is version 1.2 of the entry. See complete history


Literature

N-terminal domain of {alpha}B-crystallin provides a conformational switch for multimerization and structural heterogeneity.

Jehle, S.Vollmar, B.S.Bardiaux, B.Dove, K.K.Rajagopal, P.Gonen, T.Oschkinat, H.Klevit, R.E.

(2011) Proc Natl Acad Sci U S A 108: 6409-6414

  • DOI: https://doi.org/10.1073/pnas.1014656108
  • Primary Citation of Related Structures:  
    3J07

  • PubMed Abstract: 

    The small heat shock protein (sHSP) αB-crystallin (αB) plays a key role in the cellular protection system against stress. For decades, high-resolution structural studies on heterogeneous sHSPs have been confounded by the polydisperse nature of αB oligomers. We present an atomic-level model of full-length αB as a symmetric 24-subunit multimer based on solid-state NMR, small-angle X-ray scattering (SAXS), and EM data. The model builds on our recently reported structure of the homodimeric α-crystallin domain (ACD) and C-terminal IXI motif in the context of the multimer. A hierarchy of interactions contributes to build multimers of varying sizes: Interactions between two ACDs define a dimer, three dimers connected by their C-terminal regions define a hexameric unit, and variable interactions involving the N-terminal region define higher-order multimers. Within a multimer, N-terminal regions exist in multiple environments, contributing to the heterogeneity observed by NMR. Analysis of SAXS data allows determination of a heterogeneity parameter for this type of system. A mechanism of multimerization into higher-order asymmetric oligomers via the addition of up to six dimeric units to a 24-mer is proposed. The proposed asymmetric multimers explain the homogeneous appearance of αB in negative-stain EM images and the known dynamic exchange of αB subunits. The model of αB provides a structural basis for understanding known disease-associated missense mutations and makes predictions concerning substrate binding and the reported fibrilogenesis of αB.


  • Organizational Affiliation

    Department of Biochemistry, University of Washington, Seattle, WA 98195, USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
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 
Gene Names: CRYABCRYA2
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: SOLID-STATE NMR
  • Conformers Calculated: 200 
  • Conformers Submitted: 
  • Selection Criteria: structures with the lowest energy 
  • Method: SOLUTION SCATTERING
  • Method: ELECTRON MICROSCOPY
  • Resolution: 20.0 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 

Structure Validation

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Currently 3J07 does not have a validation slider image.



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2016-01-20
    Type: Initial release
  • Version 1.1: 2016-11-23
    Changes: Other
  • Version 1.2: 2019-04-24
    Changes: Data collection