4hse
From Proteopedia
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{{STRUCTURE_4hse| PDB=4hse | SCENE= }} | {{STRUCTURE_4hse| PDB=4hse | SCENE= }} | ||
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===Crystal structure of ClpB NBD1 in complex with guanidinium chloride and ADP=== | ===Crystal structure of ClpB NBD1 in complex with guanidinium chloride and ADP=== | ||
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{{ABSTRACT_PUBMED_23341453}} | {{ABSTRACT_PUBMED_23341453}} | ||
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| + | ==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> | ||
==About this Structure== | ==About this Structure== | ||
[[4hse]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus_hb8 Thermus thermophilus hb8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HSE OCA]. | [[4hse]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus_hb8 Thermus thermophilus hb8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HSE OCA]. | ||
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| + | ==Reference== | ||
| + | <references group="xtra"/><references/> | ||
[[Category: Thermus thermophilus hb8]] | [[Category: Thermus thermophilus hb8]] | ||
[[Category: Reinstein, J.]] | [[Category: Reinstein, J.]] | ||
Revision as of 22:43, 3 April 2013
Contents |
Crystal structure of ClpB NBD1 in complex with guanidinium chloride and ADP
Template:ABSTRACT PUBMED 23341453
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
4hse is a 1 chain structure with sequence from Thermus thermophilus hb8. Full crystallographic information is available from OCA.
