6PXI

The crystal structure of a singly capped HslUV complex with an axial pore plug and a HslU E257Q mutation

Summary for 6PXI

Entry DOI	10.2210/pdb6pxi/pdb
Descriptor	ATP-dependent protease subunit HslV, ATP-dependent protease ATPase subunit HslU, SULFATE ION, ... (5 entities in total)
Functional Keywords	aaa+ atpase, peptidase, hydrolase
Biological source	Escherichia coli More
Total number of polymer chains	6
Total formula weight	177517.64
Authors	Baytshtok, V.,Grant, R.A.,Sauer, R.T. (deposition date: 2019-07-26, release date: 2020-07-29, Last modification date: 2024-06-19)
Primary citation	Baytshtok, V.,Fei, X.,Shih, T.T.,Grant, R.A.,Santos, J.C.,Baker, T.A.,Sauer, R.T. Heat activates the AAA+ HslUV protease by melting an axial autoinhibitory plug. Cell Rep, 34:108639-108639, 2021 Cited by PubMed Abstract: At low temperatures, protein degradation by the AAA+ HslUV protease is very slow. New crystal structures reveal that residues in the intermediate domain of the HslU unfoldase can plug its axial channel, blocking productive substrate binding and subsequent unfolding, translocation, and degradation by the HslV peptidase. Biochemical experiments with wild-type and mutant enzymes support a model in which heat-induced melting of this autoinhibitory plug activates HslUV proteolysis. PubMed: 33472065 DOI: 10.1016/j.celrep.2020.108639 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (3.447 Å)

Structure validation