5JI3

HslUV complex

5JI3 の概要

• エントリーDOI: 10.2210/pdb5ji3/pdb
• 分子名称: ATP-dependent protease subunit HslV, ATP-dependent protease ATPase subunit HslU, 2'-DEOXYADENOSINE-5'-DIPHOSPHATE (3 entities in total)
• 機能のキーワード: aaa+ atpase, peptidase, hslvu, peptidase-atpase complex, hydrolase complex, hydrolase
• 由来する生物種: Escherichia coli; 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 176613.15

構造登録者

Grant, R.A.,Sauer, R.T.,Schmitz, K.R.,Baytshtok, V. (登録日: 2016-04-21, 公開日: 2016-12-07, 最終更新日: 2024-01-10)

主引用文献

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

実験手法

X-RAY DIFFRACTION (3 Å)