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- PDB-2n0k: Chemical shift assignments and structure of the alpha-crystallin ... -
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Basic information
Entry | Database: PDB / ID: 2n0k | ||||||
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Title | Chemical shift assignments and structure of the alpha-crystallin domain from human, HSPB5 | ||||||
![]() | Alpha-crystallin B chain | ||||||
![]() | METAL BINDING PROTEIN / crystallin / human / ACD / Protein | ||||||
Function / homology | ![]() microtubule polymerization or depolymerization / negative regulation of intracellular transport / apoptotic process involved in morphogenesis / cardiac myofibril / regulation of programmed cell death / tubulin complex assembly / structural constituent of eye lens / negative regulation of amyloid fibril formation / M band / lens development in camera-type eye ...microtubule polymerization or depolymerization / negative regulation of intracellular transport / apoptotic process involved in morphogenesis / cardiac myofibril / regulation of programmed cell death / tubulin complex assembly / structural constituent of eye lens / negative regulation of amyloid fibril formation / M band / lens development in camera-type eye / muscle organ development / actin filament bundle / HSF1-dependent transactivation / negative regulation of reactive oxygen species metabolic process / negative regulation of protein-containing complex assembly / stress-activated MAPK cascade / synaptic membrane / muscle contraction / response to hydrogen peroxide / negative regulation of cell growth / cellular response to gamma radiation / Z disc / unfolded protein binding / protein folding / response to estradiol / amyloid-beta binding / response to heat / protein refolding / microtubule binding / perikaryon / dendritic spine / lysosome / protein stabilization / response to hypoxia / axon / negative regulation of gene expression / negative regulation of DNA-templated transcription / protein-containing complex binding / negative regulation of apoptotic process / structural molecule activity / cell surface / protein homodimerization activity / protein-containing complex / mitochondrion / extracellular exosome / nucleoplasm / identical protein binding / nucleus / metal ion binding / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Model details | closest to the average, model1 | ||||||
![]() | Rajagopal, P. / Klevit, R.E. / Shi, L. / Baker, D. | ||||||
![]() | ![]() Title: A conserved histidine modulates HSPB5 structure to trigger chaperone activity in response to stress-related acidosis. Authors: Rajagopal, P. / Tse, E. / Borst, A.J. / Delbecq, S.P. / Shi, L. / Southworth, D.R. / Klevit, R.E. #1: Journal: J.Mol.Biol. / Year: 2009 Title: alphaB-crystallin: a hybrid solid-state/solution-state NMR investigation reveals structural aspects of the heterogeneous oligomer. Authors: Jehle, S. / van Rossum, B. / Stout, J.R. / Noguchi, S.M. / Falber, K. / Rehbein, K. / Oschkinat, H. / Klevit, R.E. / Rajagopal, P. #2: ![]() Title: Solid-state NMR and SAXS studies provide a structural basis for the activation of alphaB-crystallin oligomers. Authors: Stefan Jehle / Ponni Rajagopal / Benjamin Bardiaux / Stefan Markovic / Ronald Kühne / Joseph R Stout / Victoria A Higman / Rachel E Klevit / Barth-Jan van Rossum / Hartmut Oschkinat / ![]() Abstract: The small heat shock protein alphaB-crystallin (alphaB) contributes to cellular protection against stress. For decades, high-resolution structural studies on oligomeric alphaB have been confounded by ...The small heat shock protein alphaB-crystallin (alphaB) contributes to cellular protection against stress. For decades, high-resolution structural studies on oligomeric alphaB have been confounded by its polydisperse nature. Here, we present a structural basis of oligomer assembly and activation of the chaperone using solid-state NMR and small-angle X-ray scattering (SAXS). The basic building block is a curved dimer, with an angle of approximately 121 degrees between the planes of the beta-sandwich formed by alpha-crystallin domains. The highly conserved IXI motif covers a substrate binding site at pH 7.5. We observe a pH-dependent modulation of the interaction of the IXI motif with beta4 and beta8, consistent with a pH-dependent regulation of the chaperone function. N-terminal region residues Ser59-Trp60-Phe61 are involved in intermolecular interaction with beta3. Intermolecular restraints from NMR and volumetric restraints from SAXS were combined to calculate a model of a 24-subunit alphaB oligomer with tetrahedral symmetry. #3: ![]() Title: N-terminal domain of alphaB-crystallin provides a conformational switch for multimerization and structural heterogeneity. Authors: Stefan Jehle / Breanna S Vollmar / Benjamin Bardiaux / Katja K Dove / Ponni Rajagopal / Tamir Gonen / Hartmut Oschkinat / Rachel E Klevit / ![]() 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 ...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. | ||||||
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-Validation report
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Full document | ![]() | 1.9 MB | Display | |
Data in XML | ![]() | 201.3 KB | Display | |
Data in CIF | ![]() | 185.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Assembly
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Components
#1: Protein | Mass: 10200.497 Da / Num. of mol.: 2 / Fragment: unp residues 64-152 / Mutation: N146D Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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NMR details | Text: Solution structure was determined with NOEs and RDCs. |
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-NMR measurement
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