1xbl: Difference between revisions
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==NMR STRUCTURE OF THE J-DOMAIN (RESIDUES 2-76) IN THE ESCHERICHIA COLI N-TERMINAL FRAGMENT (RESIDUES 2-108) OF THE MOLECULAR CHAPERONE DNAJ, 20 STRUCTURES== | ==NMR STRUCTURE OF THE J-DOMAIN (RESIDUES 2-76) IN THE ESCHERICHIA COLI N-TERMINAL FRAGMENT (RESIDUES 2-108) OF THE MOLECULAR CHAPERONE DNAJ, 20 STRUCTURES== | ||
<StructureSection load='1xbl' size='340' side='right' caption='[[1xbl | <StructureSection load='1xbl' size='340' side='right'caption='[[1xbl]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1xbl]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1xbl]] 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=1XBL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XBL FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | </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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1xbl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xbl OCA], [https://pdbe.org/1xbl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xbl RCSB], [https://www.ebi.ac.uk/pdbsum/1xbl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xbl ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [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> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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==See Also== | ==See Also== | ||
*[[Heat Shock | *[[Heat Shock Protein structures|Heat Shock Protein structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Escherichia coli]] | ||
[[Category: Georgopoulos | [[Category: Large Structures]] | ||
[[Category: Pellecchia | [[Category: Georgopoulos C]] | ||
[[Category: Szyperski | [[Category: Pellecchia M]] | ||
[[Category: Wall | [[Category: Szyperski T]] | ||
[[Category: Wuthrich | [[Category: Wall D]] | ||
[[Category: Wuthrich K]] | |||