4lj7: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
{{STRUCTURE_4lj7| PDB=4lj7 | SCENE= }} | {{STRUCTURE_4lj7| PDB=4lj7 | SCENE= }} | ||
===ClpB NBD2 K601Q from T. thermophilus in complex with MANT-dADP=== | ===ClpB NBD2 K601Q from T. thermophilus in complex with MANT-dADP=== | ||
{{ABSTRACT_PUBMED_24531492}} | |||
==Function== | ==Function== | ||
| Line 9: | Line 10: | ||
==Reference== | ==Reference== | ||
<references group="xtra"/><references/> | <ref group="xtra">PMID:024531492</ref><references group="xtra"/><references/> | ||
[[Category: Barends, T R.M.]] | [[Category: Barends, T R.M.]] | ||
[[Category: Reinstein, J.]] | [[Category: Reinstein, J.]] | ||
Revision as of 05:13, 9 April 2014
ClpB NBD2 K601Q from T. thermophilus in complex with MANT-dADP
Template:ABSTRACT PUBMED 24531492
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
4lj7 is a 3 chain structure. Full crystallographic information is available from OCA.
Reference
- Zeymer C, Barends TR, Werbeck ND, Schlichting I, Reinstein J. Elements in nucleotide sensing and hydrolysis of the AAA+ disaggregation machine ClpB: a structure-based mechanistic dissection of a molecular motor. Acta Crystallogr D Biol Crystallogr. 2014 Feb;70(Pt 2):582-95. doi:, 10.1107/S1399004713030629. Epub 2014 Jan 31. PMID:24531492 doi:https://dx.doi.org/10.1107/S1399004713030629
