| Structural highlights
Function
[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.[1] [2] [3] [4] [5] [6] [7] [CLPQ_BACSU] Protease subunit of a proteasome-like degradation complex.[8]
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
Because of lattice-translocation defects, two identical but translated lattices can coexist as a single coherent mosaic block in a crystal. The observed structure in such cases is a weighted sum of two identical but translated structures, one from each lattice; the observed structure factors are a weighted vector sum of the structure factors with identical unit amplitudes but shifted phases. The correction of X-ray intensities from a single crystal containing these defects of the hybrid HslV-HslU complex, which consists of Escherichia coli HslU and Bacillus subtilis HslV (also known as CodW), is reported. When intensities are not corrected, a biologically irrelevant complex (with CodW from one lattice and HslU from another) is implied to exist. Only upon correction does a biologically functional CodW-HslU complex structure emerge.
Correction of X-ray intensities from an HslV-HslU co-crystal containing lattice-translocation defects.,Wang J, Rho SH, Park HH, Eom SH Acta Crystallogr D Biol Crystallogr. 2005 Jul;61(Pt 7):932-41. Epub 2005, Jun 24. PMID:15983416[9]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Yoo SJ, Seol JH, Shin DH, Rohrwild M, Kang MS, Tanaka K, Goldberg AL, Chung CH. Purification and characterization of the heat shock proteins HslV and HslU that form a new ATP-dependent protease in Escherichia coli. J Biol Chem. 1996 Jun 14;271(24):14035-40. PMID:8662828
- ↑ Rohrwild M, Coux O, Huang HC, Moerschell RP, Yoo SJ, Seol JH, Chung CH, Goldberg AL. HslV-HslU: A novel ATP-dependent protease complex in Escherichia coli related to the eukaryotic proteasome. Proc Natl Acad Sci U S A. 1996 Jun 11;93(12):5808-13. PMID:8650174
- ↑ Seol JH, Yoo SJ, Shin DH, Shim YK, Kang MS, Goldberg AL, Chung CH. The heat-shock protein HslVU from Escherichia coli is a protein-activated ATPase as well as an ATP-dependent proteinase. Eur J Biochem. 1997 Aug 1;247(3):1143-50. PMID:9288941
- ↑ Kanemori M, Nishihara K, Yanagi H, Yura T. Synergistic roles of HslVU and other ATP-dependent proteases in controlling in vivo turnover of sigma32 and abnormal proteins in Escherichia coli. J Bacteriol. 1997 Dec;179(23):7219-25. PMID:9393683
- ↑ Seong IS, Oh JY, Yoo SJ, Seol JH, Chung CH. ATP-dependent degradation of SulA, a cell division inhibitor, by the HslVU protease in Escherichia coli. FEBS Lett. 1999 Jul 30;456(1):211-4. PMID:10452560
- ↑ Kanemori M, Yanagi H, Yura T. Marked instability of the sigma(32) heat shock transcription factor at high temperature. Implications for heat shock regulation. J Biol Chem. 1999 Jul 30;274(31):22002-7. PMID:10419524
- ↑ Burton RE, Baker TA, Sauer RT. Nucleotide-dependent substrate recognition by the AAA+ HslUV protease. Nat Struct Mol Biol. 2005 Mar;12(3):245-51. Epub 2005 Feb 6. PMID:15696175 doi:10.1038/nsmb898
- ↑ Kang MS, Lim BK, Seong IS, Seol JH, Tanahashi N, Tanaka K, Chung CH. The ATP-dependent CodWX (HslVU) protease in Bacillus subtilis is an N-terminal serine protease. EMBO J. 2001 Feb 15;20(4):734-42. PMID:11179218 doi:http://dx.doi.org/10.1093/emboj/20.4.734
- ↑ Wang J, Rho SH, Park HH, Eom SH. Correction of X-ray intensities from an HslV-HslU co-crystal containing lattice-translocation defects. Acta Crystallogr D Biol Crystallogr. 2005 Jul;61(Pt 7):932-41. Epub 2005, Jun 24. PMID:15983416 doi:10.1107/S0907444905009546
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