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| | ==Thermus thermophilus DNAJ J- and G/F-DOMAINS== | | ==Thermus thermophilus DNAJ J- and G/F-DOMAINS== |
| - | <StructureSection load='4j7z' size='340' side='right' caption='[[4j7z]], [[Resolution|resolution]] 1.64Å' scene=''> | + | <StructureSection load='4j7z' size='340' side='right'caption='[[4j7z]], [[Resolution|resolution]] 1.64Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4j7z]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Thet8 Thet8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4J7Z OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4J7Z FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4j7z]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus_HB8 Thermus thermophilus HB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4J7Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4J7Z FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4j80|4j80]]</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=4j7z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4j7z OCA], [https://pdbe.org/4j7z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4j7z RCSB], [https://www.ebi.ac.uk/pdbsum/4j7z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4j7z 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=300852 THET8])</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=4j7z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4j7z OCA], [http://pdbe.org/4j7z PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4j7z RCSB], [http://www.ebi.ac.uk/pdbsum/4j7z PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4j7z 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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 4j7z" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 4j7z" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Heat Shock Protein structures|Heat Shock Protein structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Thet8]] | + | [[Category: Large Structures]] |
| - | [[Category: Barends, T R.M]] | + | [[Category: Thermus thermophilus HB8]] |
| - | [[Category: Bittl, R]] | + | [[Category: Barends TRM]] |
| - | [[Category: Brosi, R W]] | + | [[Category: Bittl R]] |
| - | [[Category: Eschenbach, J]] | + | [[Category: Brosi RW]] |
| - | [[Category: Hartmann, E]] | + | [[Category: Eschenbach J]] |
| - | [[Category: Lorenz, T]] | + | [[Category: Hartmann E]] |
| - | [[Category: Reinstein, J]] | + | [[Category: Lorenz T]] |
| - | [[Category: Scherer, A]] | + | [[Category: Reinstein J]] |
| - | [[Category: Schlichting, I]] | + | [[Category: Scherer A]] |
| - | [[Category: Seidel, R]] | + | [[Category: Schlichting I]] |
| - | [[Category: Shoeman, R]] | + | [[Category: Seidel R]] |
| - | [[Category: Steinmetz, A]] | + | [[Category: Shoeman R]] |
| - | [[Category: Zimmermann, S]] | + | [[Category: Steinmetz A]] |
| - | [[Category: Chaperone]]
| + | [[Category: Zimmermann S]] |
| - | [[Category: Dna replication]]
| + | |
| - | [[Category: J-domain]]
| + | |
| - | [[Category: Polyproline-ii helix]]
| + | |
| - | [[Category: Stress response]]
| + | |
| 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]
Publication Abstract from PubMed
Hsp70 chaperones assist in a large variety of protein-folding processes in the cell. Crucial for these activities is the regulation of Hsp70 by Hsp40 cochaperones. DnaJ, the bacterial homologue of Hsp40, stimulates ATP hydrolysis by DnaK (Hsp70) and thus mediates capture of substrate protein, but is also known to possess chaperone activity of its own. The first structure of a complete functional dimeric DnaJ was determined and the mobility of its individual domains in solution was investigated. Crystal structures of the complete molecular cochaperone DnaJ from Thermus thermophilus comprising the J, GF and C-terminal domains and of the J and GF domains alone showed an ordered GF domain interacting with the J domain. Structure-based EPR spin-labelling studies as well as cross-linking results showed the existence of multiple states of DnaJ in solution with different arrangements of the various domains, which has implications for the function of DnaJ.
Combining crystallography and EPR: crystal and solution structures of the multidomain cochaperone DnaJ.,Barends TR, Brosi RW, Steinmetz A, Scherer A, Hartmann E, Eschenbach J, Lorenz T, Seidel R, Shoeman RL, Zimmermann S, Bittl R, Schlichting I, Reinstein J Acta Crystallogr D Biol Crystallogr. 2013 Aug;69(Pt 8):1540-52. doi:, 10.1107/S0907444913010640. Epub 2013 Jul 19. PMID:23897477[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
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
- ↑ Barends TR, Brosi RW, Steinmetz A, Scherer A, Hartmann E, Eschenbach J, Lorenz T, Seidel R, Shoeman RL, Zimmermann S, Bittl R, Schlichting I, Reinstein J. Combining crystallography and EPR: crystal and solution structures of the multidomain cochaperone DnaJ. Acta Crystallogr D Biol Crystallogr. 2013 Aug;69(Pt 8):1540-52. doi:, 10.1107/S0907444913010640. Epub 2013 Jul 19. PMID:23897477 doi:http://dx.doi.org/10.1107/S0907444913010640
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