3ucs
From Proteopedia
(Difference between revisions)
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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=3ucs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ucs OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ucs RCSB], [http://www.ebi.ac.uk/pdbsum/3ucs PDBsum]</span></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=3ucs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ucs OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ucs RCSB], [http://www.ebi.ac.uk/pdbsum/3ucs PDBsum]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/CBPA_ECOLI CBPA_ECOLI]] DNA-binding protein that preferentially recognizes a curved DNA sequence. It is probably a functional analog of DnaJ; displays overlapping activities with DnaJ, but functions under different conditions, probably acting as a molecular chaperone in an adaptive response to environmental stresses other than heat shock. Lacks autonomous chaperone activity; binds native substrates and targets them for recognition by DnaK. Its activity is inhibited by the binding of CbpM.<ref>PMID:7601860</ref> <ref>PMID:8824642</ref> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 22:24, 25 December 2014
Crystal structure of the complex between CBPA J-domain and CBPM
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