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6prq

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Current revision (07:36, 1 May 2024) (edit) (undo)
 
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==Structural Basis for Client Recognition and Activity of Hsp40 Chaperones==
==Structural Basis for Client Recognition and Activity of Hsp40 Chaperones==
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<StructureSection load='6prq' size='340' side='right'caption='[[6prq]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
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<StructureSection load='6prq' size='340' side='right'caption='[[6prq]]' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6prq]] 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=6PRQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6PRQ FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6prq]] 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=6PRQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6PRQ FirstGlance]. <br>
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</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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<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>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6prq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6prq OCA], [https://pdbe.org/6prq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6prq RCSB], [https://www.ebi.ac.uk/pdbsum/6prq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6prq ProSAT]</span></td></tr>
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<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=6prq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6prq OCA], [http://pdbe.org/6prq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6prq RCSB], [http://www.ebi.ac.uk/pdbsum/6prq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6prq ProSAT]</span></td></tr>
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</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[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]
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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.
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 6prq" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Alkaline phosphatase]]
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[[Category: Escherichia coli K-12]]
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[[Category: Ecoli]]
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[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Jiang, Y]]
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[[Category: Thermus thermophilus HB8]]
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[[Category: Kalodimos, C G]]
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[[Category: Jiang Y]]
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[[Category: Rossi, P]]
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[[Category: Kalodimos CG]]
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[[Category: Chaperone]]
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[[Category: Rossi P]]
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[[Category: Client recognition]]
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[[Category: Hydrolase]]
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Structural Basis for Client Recognition and Activity of Hsp40 Chaperones

PDB ID 6prq

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