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460630.0 [No comment] 20.03.2013 11:45 Released

ID: 460630.0, MPI für Entwicklungsbiologie / Abteilung 1 - Protein Evolution (A. Lupas)
Structural basis of N-end rule substrate recognition in Escherichia coli by the ClpAP adaptor protein ClpS
Authors:Schuenemann, V. J.; Kralik, S. M.; Albrecht, R.; Spall, S. K.; Truscott, K. N.; Dougan, D. A.; Zeth, K.
Date of Publication (YYYY-MM-DD):2009-05
Title of Journal:EMBO Rep
Issue / Number:5
Start Page:508
End Page:514
Review Status:not specified
Audience:Not Specified
Abstract / Description: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.
Free Keywords:Amino Acid Sequence; Carrier Proteins/*chemistry/*metabolism; Endopeptidase Clp/*metabolism; Escherichia coli/*metabolism; Escherichia coli Proteins/*chemistry/*metabolism; Leucine/chemistry; Models, Biological; Molecular Sequence Data; Peptides/*chemistry/*metabolism; Phenylalanine/chemistry; Protein Binding; Protein Structure, Quaternary; Protein Structure, Tertiary; Tryptophan/chemistry
External Publication Status:published
Document Type:Article
Affiliations:MPI für Entwicklungsbiologie/Abteilung 1 - Proteinevolution (Andrei Lupas)
External Affiliations:%G eng
Identifiers:ISSN:1469-3178 (Electronic) 1469-221X (Linking) %R embo... [ID No:1]
URL:http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=... [ID No:2]