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Structural basis of N‐end rule substrate recognition in Escherichia coli by the ClpAP adaptor protein ClpS
Author(s) -
Schuenemann Verena J,
Kralik Stephanie M,
Albrecht Reinhard,
Spall Sukhdeep K,
Truscott Kaye N,
Dougan David A,
Zeth Kornelius
Publication year - 2009
Publication title -
embo reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.584
H-Index - 184
eISSN - 1469-3178
pISSN - 1469-221X
DOI - 10.1038/embor.2009.62
Subject(s) - degron , escherichia coli , signal transducing adaptor protein , biochemistry , residue (chemistry) , binding site , chemistry , proteolysis , plasma protein binding , peptide sequence , peptide , dodecameric protein , n terminus , protein structure , protease , c terminus , biology , amino acid , stereochemistry , ubiquitin , enzyme , phosphorylation , ubiquitin ligase , dna , gene
In Escherichia coli , the ClpAP protease, together with the adaptor protein ClpS, is responsible for the degradation of proteins bearing an amino‐terminal destabilizing amino acid (N‐degron). Here, we determined the three‐dimensional structures of ClpS in complex with three peptides, each having a different destabilizing residue—Leu, Phe or Trp—at its N terminus. All peptides, regardless of the identity of their N‐terminal residue, are bound in a surface pocket on ClpS in a stereo‐specific manner. Several highly conserved residues in this binding pocket interact directly with the backbone of the N‐degron peptide and hence are crucial for the binding of all N‐degrons. By contrast, two hydrophobic residues define the volume of the binding pocket and influence the specificity of ClpS. Taken together, our data suggest that ClpS has been optimized for the binding and delivery of N‐degrons containing an N‐terminal Phe or Leu.

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