3O1F

P1 crystal form of E. coli ClpS at 1.4 A resolution

Summary for 3O1F

• Entry DOI: 10.2210/pdb3o1f/pdb
• Descriptor: ATP-dependent Clp protease adapter protein clpS (3 entities in total)
• Functional Keywords: adaptor, hydrolase
• Biological source: Escherichia coli; More
• Total number of polymer chains: 2
• Total formula weight: 18595.53

Authors

Roman-Hernandez, G.,Hou, J.Y.,Grant, R.A.,Sauer, R.T.,Baker, T.A. (deposition date: 2010-07-21, release date: 2011-07-27, Last modification date: 2025-03-26)

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 (1.4 Å)