Structural highlights
Function
[CLPS_CAUCR] Involved in the modulation of the specificity of the ClpAP-mediated ATP-dependent protein degradation (By similarity).
Publication Abstract from PubMed
The N-end rule targets specific proteins for destruction in prokaryotes and eukaryotes. Here, we report a crystal structure of a bacterial N-end rule adaptor, ClpS, bound to a peptide mimic of an N-end rule substrate. This structure, which was solved at a resolution of 1.15 A, reveals specific recognition of the peptide alpha-amino group via hydrogen bonding and shows that the peptide's N-terminal tyrosine side chain is buried in a deep hydrophobic cleft that pre-exists on the surface of ClpS. The adaptor side chains that contact the peptide's N-terminal residue are highly conserved in orthologs and in E3 ubiquitin ligases that mediate eukaryotic N-end rule recognition. We show that mutation of critical ClpS contact residues abrogates substrate delivery to and degradation by the AAA+ protease ClpAP, demonstrate that modification of the hydrophobic pocket results in altered N-end rule specificity, and discuss functional implications for the mechanism of substrate delivery.
The molecular basis of N-end rule recognition.,Wang KH, Roman-Hernandez G, Grant RA, Sauer RT, Baker TA Mol Cell. 2008 Nov 7;32(3):406-14. PMID:18995838[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Wang KH, Roman-Hernandez G, Grant RA, Sauer RT, Baker TA. The molecular basis of N-end rule recognition. Mol Cell. 2008 Nov 7;32(3):406-14. PMID:18995838 doi:http://dx.doi.org/S1097-2765(08)00692-8
