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| | ==Structural Basis for Client Recognition and Activity of Hsp40 Chaperones== | | ==Structural Basis for Client Recognition and Activity of Hsp40 Chaperones== |
| - | <StructureSection load='6pri' size='340' side='right'caption='[[6pri]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='6pri' size='340' side='right'caption='[[6pri]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6pri]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6PRI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6PRI FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6pri]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12] and [https://en.wikipedia.org/wiki/Thermus_thermophilus_HB8 Thermus thermophilus HB8]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6PRI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6PRI FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6pq2|6pq2]]</td></tr> | + | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6pri FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6pri OCA], [https://pdbe.org/6pri PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6pri RCSB], [https://www.ebi.ac.uk/pdbsum/6pri PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6pri ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">dnaJ2, TTHA1489 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr>
| + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Alkaline_phosphatase Alkaline phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.1 3.1.3.1] </span></td></tr>
| + | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6pri FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6pri OCA], [http://pdbe.org/6pri PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6pri RCSB], [http://www.ebi.ac.uk/pdbsum/6pri PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6pri ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/DNAJ2_THET8 DNAJ2_THET8] Does not influence ATP binding or hydrolysis nor ADP release. Exerts influence on the interaction of DnaK with substrates; in the presence of DafA, DnaJ inhibits substrate binding, and substrate already bound to DnaK is displaced by DnaJ and DafA.<ref>PMID:10092456</ref> [https://www.uniprot.org/uniprot/PPB_ECOLI PPB_ECOLI] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Alkaline phosphatase]] | + | [[Category: Escherichia coli K-12]] |
| - | [[Category: Ecoli]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Jiang, Y]] | + | [[Category: Thermus thermophilus HB8]] |
| - | [[Category: Kalodimos, C G]] | + | [[Category: Jiang Y]] |
| - | [[Category: Rossi, P]] | + | [[Category: Kalodimos CG]] |
| - | [[Category: Chaperone]] | + | [[Category: Rossi P]] |
| - | [[Category: Chaperone-hydrolase complex]]
| + | |
| - | [[Category: Client recognition]]
| + | |
| Structural highlights
Function
DNAJ2_THET8 Does not influence ATP binding or hydrolysis nor ADP release. Exerts influence on the interaction of DnaK with substrates; in the presence of DafA, DnaJ inhibits substrate binding, and substrate already bound to DnaK is displaced by DnaJ and DafA.[1] PPB_ECOLI
Publication Abstract from PubMed
Hsp70 and Hsp40 chaperones work synergistically in a wide range of biological processes including protein synthesis, membrane translocation, and folding. We used nuclear magnetic resonance spectroscopy to determine the solution structure and dynamic features of an Hsp40 in complex with an unfolded client protein. Atomic structures of the various binding sites in the client complexed to the binding domains of the Hsp40 reveal the recognition pattern. Hsp40 engages the client in a highly dynamic fashion using a multivalent binding mechanism that alters the folding properties of the client. Different Hsp40 family members have different numbers of client-binding sites with distinct sequence selectivity, providing additional mechanisms for activity regulation and function modification. Hsp70 binding to Hsp40 displaces the unfolded client. The activity of Hsp40 is altered in its complex with Hsp70, further regulating client binding and release.
Structural basis for client recognition and activity of Hsp40 chaperones.,Jiang Y, Rossi P, Kalodimos CG Science. 2019 Sep 20;365(6459):1313-1319. doi: 10.1126/science.aax1280. PMID:31604242[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Klostermeier D, Seidel R, Reinstein J. The functional cycle and regulation of the Thermus thermophilus DnaK chaperone system. J Mol Biol. 1999 Apr 2;287(3):511-25. PMID:10092456 doi:10.1006/jmbi.1999.2636
- ↑ Jiang Y, Rossi P, Kalodimos CG. Structural basis for client recognition and activity of Hsp40 chaperones. Science. 2019 Sep 20;365(6459):1313-1319. doi: 10.1126/science.aax1280. PMID:31604242 doi:http://dx.doi.org/10.1126/science.aax1280
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