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Yorodumi- PDB-7zhs: 3D reconstruction of the cylindrical assembly of DnaJA2 delta G/F... -
+Open data
-Basic information
Entry | Database: PDB / ID: 7zhs | |||||||||
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Title | 3D reconstruction of the cylindrical assembly of DnaJA2 delta G/F by imposing D5 symmetry | |||||||||
Components | Ubiquitin-like protein SMT3,DnaJ homolog subfamily A member 2 | |||||||||
Keywords | CHAPERONE / oligomer / filaments / helix / holdase / foldase / Hsp40 / DnaJA2 / Hsp70 co-chaperone | |||||||||
Function / homology | Function and homology information SUMO is conjugated to E1 (UBA2:SAE1) / SUMOylation of nuclear envelope proteins / SUMO is transferred from E1 to E2 (UBE2I, UBC9) / SUMO is proteolytically processed / SUMOylation of transcription factors / Postmitotic nuclear pore complex (NPC) reformation / SUMOylation of transcription cofactors / septin ring / SUMOylation of DNA damage response and repair proteins / SUMOylation of DNA replication proteins ...SUMO is conjugated to E1 (UBA2:SAE1) / SUMOylation of nuclear envelope proteins / SUMO is transferred from E1 to E2 (UBE2I, UBC9) / SUMO is proteolytically processed / SUMOylation of transcription factors / Postmitotic nuclear pore complex (NPC) reformation / SUMOylation of transcription cofactors / septin ring / SUMOylation of DNA damage response and repair proteins / SUMOylation of DNA replication proteins / Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks / SUMOylation of SUMOylation proteins / SUMOylation of RNA binding proteins / SUMOylation of chromatin organization proteins / ubiquitin-like protein ligase binding / ATPase activator activity / protein sumoylation / HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand / Hsp70 protein binding / condensed nuclear chromosome / protein tag activity / unfolded protein binding / protein-folding chaperone binding / response to heat / protein refolding / positive regulation of cell population proliferation / extracellular exosome / ATP binding / identical protein binding / membrane / nucleus / metal ion binding / cytosol / cytoplasm Similarity search - Function | |||||||||
Biological species | Saccharomyces cerevisiae S288c (yeast) Homo sapiens (human) | |||||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 6.9 Å | |||||||||
Authors | Cuellar, J. / Velasco-Carneros, L. / Santiago, C. / Martin-Benito, J. / Valpuesta, J. / Muga, A. | |||||||||
Funding support | Spain, 2items
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Citation | Journal: Nat Commun / Year: 2023 Title: The self-association equilibrium of DNAJA2 regulates its interaction with unfolded substrate proteins and with Hsc70. Authors: Lorea Velasco-Carneros / Jorge Cuéllar / Leire Dublang / César Santiago / Jean-Didier Maréchal / Jaime Martín-Benito / Moisés Maestro / José Ángel Fernández-Higuero / Natalia Orozco ...Authors: Lorea Velasco-Carneros / Jorge Cuéllar / Leire Dublang / César Santiago / Jean-Didier Maréchal / Jaime Martín-Benito / Moisés Maestro / José Ángel Fernández-Higuero / Natalia Orozco / Fernando Moro / José María Valpuesta / Arturo Muga / Abstract: J-domain proteins tune the specificity of Hsp70s, engaging them in precise functions. Despite their essential role, the structure and function of many J-domain proteins remain largely unknown. We ...J-domain proteins tune the specificity of Hsp70s, engaging them in precise functions. Despite their essential role, the structure and function of many J-domain proteins remain largely unknown. We explore human DNAJA2, finding that it reversibly forms highly-ordered, tubular structures that can be dissociated by Hsc70, the constitutively expressed Hsp70 isoform. Cryoelectron microscopy and mutational studies reveal that different domains are involved in self-association. Oligomer dissociation into dimers potentiates its interaction with unfolded client proteins. The J-domains are accessible to Hsc70 within the tubular structure. They allow binding of closely spaced Hsc70 molecules that could be transferred to the unfolded substrate for its cooperative remodelling, explaining the efficient recovery of DNAJA2-bound clients. The disordered C-terminal domain, comprising the last 52 residues, regulates its holding activity and productive interaction with Hsc70. These in vitro findings suggest that the association equilibrium of DNAJA2 could regulate its interaction with client proteins and Hsc70. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 7zhs.cif.gz | 1.7 MB | Display | PDBx/mmCIF format |
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PDB format | pdb7zhs.ent.gz | 1.3 MB | Display | PDB format |
PDBx/mmJSON format | 7zhs.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 7zhs_validation.pdf.gz | 1.5 MB | Display | wwPDB validaton report |
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Full document | 7zhs_full_validation.pdf.gz | 1.5 MB | Display | |
Data in XML | 7zhs_validation.xml.gz | 191.1 KB | Display | |
Data in CIF | 7zhs_validation.cif.gz | 280.3 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/zh/7zhs ftp://data.pdbj.org/pub/pdb/validation_reports/zh/7zhs | HTTPS FTP |
-Related structure data
Related structure data | 14736MC M: map data used to model this data C: citing same article (ref.) |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
-Assembly
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Noncrystallographic symmetry (NCS) | NCS domain:
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