1exk

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{{Seed}}
 
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[[Image:1exk.png|left|200px]]
 
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==SOLUTION STRUCTURE OF THE CYSTEINE-RICH DOMAIN OF THE ESCHERICHIA COLI CHAPERONE PROTEIN DNAJ.==
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The line below this paragraph, containing "STRUCTURE_1exk", creates the "Structure Box" on the page.
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<StructureSection load='1exk' size='340' side='right'caption='[[1exk]]' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1exk]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EXK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EXK FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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{{STRUCTURE_1exk| PDB=1exk | SCENE= }}
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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=1exk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1exk OCA], [https://pdbe.org/1exk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1exk RCSB], [https://www.ebi.ac.uk/pdbsum/1exk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1exk ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/DNAJ_ECOLI DNAJ_ECOLI] Interacts with DnaK and GrpE to disassemble a protein complex at the origins of replication of phage lambda and several plasmids. Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.<ref>PMID:1826368</ref> <ref>PMID:15302880</ref> <ref>PMID:15044009</ref> <ref>PMID:15485812</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ex/1exk_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1exk ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The solution structure of the cysteine-rich (CR) domain of Escherichia coli DnaJ has been solved by NMR methods. The structure of a 79 residue CR domain construct shows a novel fold with an overall V-shaped extended beta-hairpin topology. The CR domain is characterized by four C-X-X-C-X-G-X-G sequence motifs that bind two zinc ions. Residues in these two zinc modules show strong similarities in the grouping of resonances in the (15)N-(1)H HSQC spectrum and display pseudo-symmetry of the motifs in the calculated structures. The conformation of the cysteine residues coordinated to the zinc ion resembles that of the rubredoxin-knuckle, but there are significant differences in hydrogen bonding patterns in the two motifs. Zinc (15)N-(1)H HSQC titrations indicate that the fold of the isolated DnaJ CR domain is zinc-dependent and that one zinc module folds before the other. The C-X-X-C-X-G-X-G sequence motif is highly conserved in CR domains from a wide variety of species. The three-dimensional structure of the E. coli CR domain indicates that this sequence conservation is likely to result in a conserved structural motif.
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===SOLUTION STRUCTURE OF THE CYSTEINE-RICH DOMAIN OF THE ESCHERICHIA COLI CHAPERONE PROTEIN DNAJ.===
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Solution structure of the cysteine-rich domain of the Escherichia coli chaperone protein DnaJ.,Martinez-Yamout M, Legge GB, Zhang O, Wright PE, Dyson HJ J Mol Biol. 2000 Jul 21;300(4):805-18. PMID:10891270<ref>PMID:10891270</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 1exk" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_10891270}}, adds the Publication Abstract to the page
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*[[Heat Shock Protein structures|Heat Shock Protein structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 10891270 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_10891270}}
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__TOC__
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</StructureSection>
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==About this Structure==
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1EXK is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EXK OCA].
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==Reference==
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Solution structure of the cysteine-rich domain of the Escherichia coli chaperone protein DnaJ., Martinez-Yamout M, Legge GB, Zhang O, Wright PE, Dyson HJ, J Mol Biol. 2000 Jul 21;300(4):805-18. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10891270 10891270]
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Dyson, H J.]]
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[[Category: Dyson HJ]]
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[[Category: Legge, G B.]]
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[[Category: Legge GB]]
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[[Category: Martinez-Yamout, M.]]
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[[Category: Martinez-Yamout M]]
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[[Category: Wright, P E.]]
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[[Category: Wright PE]]
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[[Category: Zhang, O.]]
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[[Category: Zhang O]]
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[[Category: Cxxcxgxg]]
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[[Category: Extended beta-hairpin]]
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[[Category: Zinc-binding motif]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 02:10:31 2008''
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Current revision

SOLUTION STRUCTURE OF THE CYSTEINE-RICH DOMAIN OF THE ESCHERICHIA COLI CHAPERONE PROTEIN DNAJ.

PDB ID 1exk

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