5JI3

HslUV complex

Summary for 5JI3

• Entry DOI: 10.2210/pdb5ji3/pdb
• Descriptor: ATP-dependent protease subunit HslV, ATP-dependent protease ATPase subunit HslU, 2'-DEOXYADENOSINE-5'-DIPHOSPHATE (3 entities in total)
• Functional Keywords: aaa+ atpase, peptidase, hslvu, peptidase-atpase complex, hydrolase complex, hydrolase
• Biological source: Escherichia coli; More
• Total number of polymer chains: 6
• Total formula weight: 176613.15

Authors

Grant, R.A.,Sauer, R.T.,Schmitz, K.R.,Baytshtok, V. (deposition date: 2016-04-21, release date: 2016-12-07, Last modification date: 2024-01-10)

Primary citation

Baytshtok, V.,Fei, X.,Grant, R.A.,Baker, T.A.,Sauer, R.T.
A Structurally Dynamic Region of the HslU Intermediate Domain Controls Protein Degradation and ATP Hydrolysis.
Structure, 24:1766-1777, 2016

PubMed Abstract: The I domain of HslU sits above the AAA+ ring and forms a funnel-like entry to the axial pore, where protein substrates are engaged, unfolded, and translocated into HslV for degradation. The L199Q I-domain substitution, which was originally reported as a loss-of-function mutation, resides in a segment that appears to adopt multiple conformations as electron density is not observed in HslU and HslUV crystal structures. The L199Q sequence change does not alter the structure of the AAA+ ring or its interactions with HslV but increases I-domain susceptibility to limited endoproteolysis. Notably, the L199Q mutation increases the rate of ATP hydrolysis substantially, results in slower degradation of some proteins but faster degradation of other substrates, and markedly changes the preference of HslUV for initiating degradation at the N or C terminus of model substrates. Thus, a structurally dynamic region of the I domain plays a key role in controlling protein degradation by HslUV.

PubMed: 27667691
DOI: 10.1016/j.str.2016.08.012

Experimental method

X-RAY DIFFRACTION (3 Å)