3O2B

E. coli ClpS in complex with a Phe N-end rule peptide

Summary for 3O2B

• Entry DOI: 10.2210/pdb3o2b/pdb
• Related: 3O1F 3O2B 3O2O
• Descriptor: ATP-dependent Clp protease adaptor protein ClpS, Phe N-end rule peptide, SULFATE ION, ... (5 entities in total)
• Functional Keywords: adaptor, protein-peptide complex, peptide-binding protein, n-end rule peptide, peptide binding protein
• Biological source: Escherichia coli
• Total number of polymer chains: 4
• Total formula weight: 26685.91

Authors

Roman-Hernandez, G.,Grant, R.A.,Sauer, R.T.,Baker, T.A.,de Regt, A. (deposition date: 2010-07-22, release date: 2011-12-14, Last modification date: 2024-02-21)

Primary citation

Roman-Hernandez, G.,Hou, J.Y.,Grant, R.A.,Sauer, R.T.,Baker, T.A.
The ClpS adaptor mediates staged delivery of N-end rule substrates to the AAA+ ClpAP protease.
Mol.Cell, 43:217-228, 2011

PubMed Abstract: The ClpS adaptor delivers N-end rule substrates to ClpAP, an energy-dependent AAA+ protease, for degradation. How ClpS binds specific N-end residues is known in atomic detail and clarified here, but the delivery mechanism is poorly understood. We show that substrate binding is enhanced when ClpS binds hexameric ClpA. Reciprocally, N-end rule substrates increase ClpS affinity for ClpA(6). Enhanced binding requires the N-end residue and a peptide bond of the substrate, as well as multiple aspects of ClpS, including a side chain that contacts the substrate α-amino group and the flexible N-terminal extension (NTE). Finally, enhancement also needs the N domain and AAA+ rings of ClpA, connected by a long linker. The NTE can be engaged by the ClpA translocation pore, but ClpS resists unfolding/degradation. We propose a staged-delivery model that illustrates how intimate contacts between the substrate, adaptor, and protease reprogram specificity and coordinate handoff from the adaptor to the protease.

PubMed: 21777811
DOI: 10.1016/j.molcel.2011.06.009

Experimental method

X-RAY DIFFRACTION (2.05 Å)