ATP-dependent Clp protease adaptor protein: Difference between revisions
Michal Harel (talk | contribs) New page: <StructureSection load='3o2h' size='340' side='right' caption='E. coli ClpS complex with peptide (PDB code 3o2h)' scene=''> == Function == '''ATP-dependent Clp protease adaptor pro... |
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<StructureSection load='3o2h' size='340' side='right' caption='E. coli ClpS (grey) complex with peptide (green) (PDB code [[3o2h]])' scene=''> | |||
<StructureSection load='3o2h' size='340' side='right' caption='E. coli ClpS complex with peptide (PDB code [[3o2h]])' scene=''> | |||
== Function == | == Function == | ||
'''ATP-dependent Clp protease adaptor protein''' (ClpS) influences the protein degradation by binding to the chaperone-protease ClpAP toward degradation of aggregated proteins<ref>PMID:11931773</ref>. | '''ATP-dependent Clp protease adaptor protein''' (ClpS) influences the protein degradation by binding to the chaperone-protease ClpAP toward degradation of aggregated proteins<ref>PMID:11931773</ref>. Degradation susceptibility is related to N-terminal residues. It is formulated by the N-end rule<ref>PMID:18708349</ref>. In bacteria the residues are Tyr, Phe, Trp and Leu. ClpS binds these residues and delivers the protein to degradation by ClpAP<ref>PMID:19373253</ref>. | ||
== Structural highlights == | == Structural highlights == | ||
ClpS His residue binds to the N-terminal Leu which is one of the N-end rule residues<ref>PMID:11931773</ref>. | |||
</StructureSection> | </StructureSection> | ||