1YFN

Versatile modes of peptide recognition by the AAA+ adaptor protein SspB- the crystal structure of a SspB-RseA complex

Summary for 1YFN

• Entry DOI: 10.2210/pdb1yfn/pdb
• Related: 1OU8 1OU9 1OUL 1OX8 1OX9
• Descriptor: Stringent starvation protein B, Sigma-E factor negative regulatory protein (3 entities in total)
• Functional Keywords: protein-peptide complex, sspb, rsea, protein binding
• Biological source: Escherichia coli; More
• Cellular location: Cell membrane; Single-pass membrane protein (Potential): P38106
• Total number of polymer chains: 8
• Total formula weight: 67564.98

Authors

Levchenko, I.,Grant, R.A.,Flynn, J.M.,Sauer, R.T.,Baker, T.A. (deposition date: 2005-01-03, release date: 2005-05-17, Last modification date: 2023-08-23)

Primary citation

Levchenko, I.,Grant, R.A.,Flynn, J.M.,Sauer, R.T.,Baker, T.A.
Versatile modes of peptide recognition by the AAA+ adaptor protein SspB
Nat.Struct.Mol.Biol., 12:520-525, 2005

PubMed Abstract: Energy-dependent proteases often rely on adaptor proteins to modulate substrate recognition. The SspB adaptor binds peptide sequences in the stress-response regulator RseA and in ssrA-tagged proteins and delivers these molecules to the AAA+ ClpXP protease for degradation. The structure of SspB bound to an ssrA peptide is known. Here, we report the crystal structure of a complex between SspB and its recognition peptide in RseA. Notably, the RseA sequence is positioned in the peptide-binding groove of SspB in a direction opposite to the ssrA peptide, the two peptides share only one common interaction with the adaptor, and the RseA interaction site is substantially larger than the overlapping ssrA site. This marked diversity in SspB recognition of different target proteins indicates that it is capable of highly flexible and dynamic substrate delivery.

PubMed: 15880122
DOI: 10.1038/nsmb934

Experimental method

X-RAY DIFFRACTION (1.8 Å)