6PXL

3.74 Angstroms resolution structure of HlsU with an axial-channel plug

Summary for 6PXL

• Entry DOI: 10.2210/pdb6pxl/pdb
• Descriptor: ATP-dependent protease ATPase subunit HslU, ADENOSINE-5'-DIPHOSPHATE, SULFATE ION, ... (4 entities in total)
• Functional Keywords: aaa+ atpase, peptidase, hydrolase
• Biological source: Escherichia coli
• Total number of polymer chains: 12
• Total formula weight: 616995.60

Authors

Baytshtok, V.,Grant, R.A.,Sauer, R.T. (deposition date: 2019-07-26, release date: 2020-07-29, Last modification date: 2024-10-23)

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

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

Experimental method

X-RAY DIFFRACTION (3.741 Å)