4lj4

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'''Unreleased structure'''
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{{STRUCTURE_4lj4| PDB=4lj4 | SCENE= }}
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===ClpB NBD2 from T. thermophilus, nucleotide-free===
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The entry 4lj4 is ON HOLD until Paper Publication
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==Function==
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[[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>
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Authors: Zeymer, C., Barends, T.R.M., Werbeck, N.D., Schlichting, I., Reinstein, J.
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==About this Structure==
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[[4lj4]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LJ4 OCA].
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Description: ClpB NBD2 from T. thermophilus, nucleotide-free
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==Reference==
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<references group="xtra"/><references/>
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[[Category: Barends, T R.M.]]
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[[Category: Reinstein, J.]]
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[[Category: Schlichting, I.]]
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[[Category: Werbeck, N D.]]
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[[Category: Zeymer, C.]]
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[[Category: Aaa+ protein]]
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[[Category: Chaperone]]
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[[Category: Disaggregase]]
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[[Category: Molecular chaperone]]
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[[Category: Nucleotide binding domain]]

Revision as of 05:19, 13 February 2014

Template:STRUCTURE 4lj4

Contents

ClpB NBD2 from T. thermophilus, nucleotide-free

Function

[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 Structure

4lj4 is a 1 chain structure. Full crystallographic information is available from OCA.

Reference

  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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OCA

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