6PXK

3.65 Angstroms resolution structure of HslU with an axial-channel plug

Summary for 6PXK

Entry DOI	10.2210/pdb6pxk/pdb
Descriptor	ATP-dependent protease ATPase subunit HslU, unidentified alpha helical sequence, ADENOSINE-5'-DIPHOSPHATE, ... (4 entities in total)
Functional Keywords	aaa+ atpase, peptidase, hydrolase
Biological source	Escherichia coli More
Total number of polymer chains	13
Total formula weight	619647.26
Authors	Baytshtok, V.,Grant, R.A.,Sauer, R.T. (deposition date: 2019-07-26, release date: 2020-07-29, Last modification date: 2024-11-06)
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 (3.647 Å)

Structure validation