4lj6: Difference between revisions

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'''Unreleased structure'''
{{STRUCTURE_4lj6|  PDB=4lj6  |  SCENE=  }}
===ClpB NBD2 from T. thermophilus in complex with AMPPCP===


The entry 4lj6 is ON HOLD until Paper Publication
==Function==
[[http://www.uniprot.org/uniprot/CLPB_THET8 CLPB_THET8]] Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK.<ref>PMID:10377389</ref>  


Authors: Zeymer, C., Barends, T.R.M., Werbeck, N.D., Schlichting, I., Reinstein, J.
==About this Structure==
[[4lj6]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LJ6 OCA].  


Description: ClpB NBD2 from T. thermophilus in complex with AMPPCP
==Reference==
<references group="xtra"/><references/>
[[Category: Barends, T R.M.]]
[[Category: Reinstein, J.]]
[[Category: Schlichting, I.]]
[[Category: Werbeck, N D.]]
[[Category: Zeymer, C.]]
[[Category: Aaa+ protein]]
[[Category: Chaperone]]
[[Category: Disaggregase]]
[[Category: Molecular chaperone]]
[[Category: Nucleotide binding domain]]

Revision as of 08:19, 13 February 2014

Template:STRUCTURE 4lj6

ClpB NBD2 from T. thermophilus in complex with AMPPCPClpB NBD2 from T. thermophilus in complex with AMPPCP

FunctionFunction

[CLPB_THET8] Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK.[1]

About this StructureAbout this Structure

4lj6 is a 1 chain structure. Full crystallographic information is available from OCA.

ReferenceReference

  1. ↑ Motohashi K, Watanabe Y, Yohda M, Yoshida M. Heat-inactivated proteins are rescued by the DnaK.J-GrpE set and ClpB chaperones. Proc Natl Acad Sci U S A. 1999 Jun 22;96(13):7184-9. PMID:10377389

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