3DNJ

The structure of the Caulobacter crescentus ClpS protease adaptor protein in complex with a N-end rule peptide

Summary for 3DNJ

• Entry DOI: 10.2210/pdb3dnj/pdb
• Descriptor: ATP-dependent Clp protease adapter protein clpS, synthetic N-end rule peptide, MAGNESIUM ION, ... (4 entities in total)
• Functional Keywords: adaptor, protein-peptide complex, peptide binding protein
• Biological source: Caulobacter vibrioides (Caulobacter vibrioides); More
• Total number of polymer chains: 4
• Total formula weight: 22485.86

Authors

Wang, K.,Roman-Hernandez, G.,Grant, R.A.,Sauer, R.T.,Baker, T.A. (deposition date: 2008-07-02, release date: 2008-11-18, Last modification date: 2024-04-03)

Primary citation

Wang, K.H.,Roman-Hernandez, G.,Grant, R.A.,Sauer, R.T.,Baker, T.A.
The molecular basis of N-end rule recognition.
Mol.Cell, 32:406-414, 2008

PubMed Abstract: 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.

PubMed: 18995838
DOI: 10.1016/j.molcel.2008.08.032

Experimental method

X-RAY DIFFRACTION (1.15 Å)