1E94

HslV-HslU from E.coli

「1DOO」から置き換えられました

1E94 の概要

• エントリーDOI: 10.2210/pdb1e94/pdb
• 関連するPDBエントリー: 1DO0 1DO2 1NED
• 分子名称: HEAT SHOCK PROTEIN HSLV, HEAT SHOCK PROTEIN HSLU, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, ... (4 entities in total)
• 機能のキーワード: chaperone, hslvu, clpqy, aaa-atpase, atp-dependent proteolysis, proteasome
• 由来する生物種: ESCHERICHIA COLI; 詳細
• 細胞内の位置: Cytoplasm: P31059
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 177950.02

構造登録者

Song, H.K.,Hartmann, C.,Ravishankar, R.,Bochtler, M. (登録日: 2000-10-07, 公開日: 2000-11-17, 最終更新日: 2023-12-13)

主引用文献

Song, H.K.,Hartmann, C.,Ravishankar, R.,Bochtler, M.,Behrendt, R.,Moroder, L.,Huber, R.
Mutational Studies on Hslu and its Docking Mode with Hslv
Proc.Natl.Acad.Sci.USA, 97:14103-, 2000

PubMed Abstract: HslVU is an ATP-dependent prokaryotic protease complex. Despite detailed crystal and molecular structure determinations of free HslV and HslU, the mechanism of ATP-dependent peptide and protein hydrolysis remained unclear, mainly because the productive complex of HslV and HslU could not be unambiguously identified from the crystal data. In the crystalline complex, the I domains of HslU interact with HslV. Observations based on electron microscopy data were interpreted in the light of the crystal structure to indicate an alternative mode of association with the intermediate domains away from HslV. By generation and analysis of two dozen HslU mutants, we find that the amidolytic and caseinolytic activities of HslVU are quite robust to mutations on both alternative docking surfaces on HslU. In contrast, HslVU activity against the maltose-binding protein-SulA fusion protein depends on the presence of the I domain and is also sensitive to mutations in the N-terminal and C-terminal domains of HslU. Mutational studies around the hexameric pore of HslU seem to show that it is involved in the recognition/translocation of maltose-binding protein-SulA but not of chromogenic small substrates and casein. ATP-binding site mutations, among other things, confirm the essential role of the "sensor arginine" (R393) and the "arginine finger" (R325) in the ATPase action of HslU and demonstrate an important role for E321. Additionally, we report a better refined structure of the HslVU complex crystallized along with resorufin-labeled casein.

PubMed: 11114186
DOI: 10.1073/PNAS.250491797

実験手法

X-RAY DIFFRACTION (2.8 Å)