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5nro

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Current revision (12:04, 22 November 2023) (edit) (undo)
 
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<StructureSection load='5nro' size='340' side='right'caption='[[5nro]], [[Resolution|resolution]] 3.25&Aring;' scene=''>
<StructureSection load='5nro' size='340' side='right'caption='[[5nro]], [[Resolution|resolution]] 3.25&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5nro]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NRO OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5NRO FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5nro]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NRO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5NRO FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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">X-ray diffraction, [[Resolution|Resolution]] 3.25&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5nro FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nro OCA], [http://pdbe.org/5nro PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5nro RCSB], [http://www.ebi.ac.uk/pdbsum/5nro PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5nro ProSAT]</span></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=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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=5nro FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nro OCA], [https://pdbe.org/5nro PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5nro RCSB], [https://www.ebi.ac.uk/pdbsum/5nro PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5nro ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/DNAK_ECOLI DNAK_ECOLI]] Plays an essential role in the initiation of phage lambda DNA replication, where it acts in an ATP-dependent fashion with the DnaJ protein to release lambda O and P proteins from the preprimosomal complex. DnaK is also involved in chromosomal DNA replication, possibly through an analogous interaction with the DnaA protein. Also participates actively in the response to hyperosmotic shock.[HAMAP-Rule:MF_00332] [[http://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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[https://www.uniprot.org/uniprot/DNAK_ECOLI DNAK_ECOLI] Plays an essential role in the initiation of phage lambda DNA replication, where it acts in an ATP-dependent fashion with the DnaJ protein to release lambda O and P proteins from the preprimosomal complex. DnaK is also involved in chromosomal DNA replication, possibly through an analogous interaction with the DnaA protein. Also participates actively in the response to hyperosmotic shock.[HAMAP-Rule:MF_00332]
<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>
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[[Category: Escherichia coli]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Kityk, R]]
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[[Category: Kityk R]]
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[[Category: Kopp, J]]
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[[Category: Kopp J]]
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[[Category: Mayer, M P]]
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[[Category: Mayer MP]]
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[[Category: Chaperone]]
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[[Category: Dnaj]]
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[[Category: Dnak]]
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[[Category: Hsp40]]
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[[Category: Hsp70]]
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Current revision

Structure of full-length DnaK with bound J-domain

PDB ID 5nro

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