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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='6psi' size='340' side='right'caption='[[6psi]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
<StructureSection load='6psi' size='340' side='right'caption='[[6psi]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6psi]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895] and [http://en.wikipedia.org/wiki/Thet8 Thet8]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6PSI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6PSI FirstGlance]. <br>
<table><tr><td colspan='2'>[[6psi]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] 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=6PSI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6PSI FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6ppt|6ppt]]</td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=300852 THET8]), phoA, ACU57_12080, AUQ13_18595, BANRA_02023, BANRA_03586, BET08_14335, BHF46_20915, BUE81_15475, C4J69_09555, C5N07_12695, CA593_01230, D0X26_07375, D3821_12940, DNQ41_05820, EAI52_02910, EC3234A_4c00530, EC3426_01222, ECTO6_03716, ED648_16735, EEP23_01005, EL75_3367, EL79_3462, EL80_3416, NCTC13462_01945, NCTC9037_03964, NCTC9062_04458, RK56_026750, SAMEA3753300_00450, UN91_18770 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</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=6psi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6psi OCA], [https://pdbe.org/6psi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6psi RCSB], [https://www.ebi.ac.uk/pdbsum/6psi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6psi ProSAT]</span></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=6psi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6psi OCA], [http://pdbe.org/6psi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6psi RCSB], [http://www.ebi.ac.uk/pdbsum/6psi PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6psi ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://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/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>  
<div style="background-color:#fffaf0;">
== 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<ref>PMID:31604242</ref>
==See Also==
 
*[[Alkaline phosphatase 3D structures|Alkaline phosphatase 3D structures]]
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
*[[Heat Shock Protein structures|Heat Shock Protein structures]]
</div>
<div class="pdbe-citations 6psi" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Bacillus coli migula 1895]]
[[Category: Escherichia coli]]
[[Category: Alkaline phosphatase]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Thet8]]
[[Category: Thermus thermophilus HB8]]
[[Category: Jiang, Y]]
[[Category: Jiang Y]]
[[Category: Kalodimos, C G]]
[[Category: Kalodimos CG]]
[[Category: Rossi, P]]
[[Category: Rossi P]]
[[Category: Chaperone]]
[[Category: Client recognition]]

Latest revision as of 10:36, 1 May 2024

Structural Basis for Client Recognition and Activity of Hsp40 ChaperonesStructural Basis for Client Recognition and Activity of Hsp40 Chaperones

Structural highlights

6psi is a 3 chain structure with sequence from Escherichia coli and Thermus thermophilus HB8. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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]

See Also

References

  1. ↑ 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
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