1e94 | pdb_00001e94

HslV-HslU from E.coli

spinqualitylabelsall models 1e94, resolution 2.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1e94 is a 6 chain structure with sequence from Ecobd. This structure supersedes the now removed PDB entry 1doo. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ANP Related: 1ned, 1do0, 1do2 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [HSLV_ECOLI] Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. The complex has been shown to be involved in the specific degradation of heat shock induced transcription factors such as RpoH and SulA. In addition, small hydrophobic peptides are also hydrolyzed by HslV. HslV has weak protease activity even in the absence of HslU, but this activity is induced more than 100-fold in the presence of HslU. HslU recognizes protein substrates and unfolds these before guiding them to HslV for hydrolysis. HslV is not believed to degrade folded proteins. [HSLU_ECOLI] ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. Mutational studies on HslU and its docking mode with HslV.,Song HK, Hartmann C, Ramachandran R, Bochtler M, Behrendt R, Moroder L, Huber R Proc Natl Acad Sci U S A. 2000 Dec 19;97(26):14103-8. PMID:11114186 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Heat Shock Protein structures

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