Gene Symbol: hslU
Description: ATP-dependent protease ATP-binding subunit HslU
Species: Haemophilus influenzae Rd KW20
Sousa M, McKay D. Structure of Haemophilus influenzae HslV protein at 1.9 A resolution, revealing a cation-binding site near the catalytic site. Acta Crystallogr D Biol Crystallogr. 2001;57:1950-4 pubmed
..The site also binds Na(+) ions and is likely to bind Mg(2+), suggesting that monovalent and divalent metal ions may influence the catalytic activity of the protease. ..
Kwon A, Trame C, McKay D. Kinetics of protein substrate degradation by HslUV. J Struct Biol. 2004;146:141-7 pubmed
..Current models propose that the HslU chaperone, a AAA protein of the Clp/Hsp100 family, binds and unfolds substrates and translocates the polypeptide ..
Song H, Hartmann C, Ramachandran R, Bochtler M, Behrendt R, Moroder L, et al
. Mutational studies on HslU and its docking mode with HslV. Proc Natl Acad Sci U S A. 2000;97:14103-8 pubmed publisher
..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 ..
Bochtler M, Hartmann C, Song H, Bourenkov G, Bartunik H, Huber R. The structures of HsIU and the ATP-dependent protease HsIU-HsIV. Nature. 2000;403:800-5 pubmed publisher
..b>HslU is a member of the Hsp100 (Clp) family of ATPases...
Sousa M, Kessler B, Overkleeft H, McKay D. Crystal structure of HslUV complexed with a vinyl sulfone inhibitor: corroboration of a proposed mechanism of allosteric activation of HslV by HslU. J Mol Biol. 2002;318:779-85 pubmed publisher
..the structure of a HslUV complex, a mechanism of allosteric activation of the HslV protease, wherein binding of the HslU chaperone propagates a conformational change to the active site cleft of the protease, has been proposed...
Sousa M, Trame C, Tsuruta H, Wilbanks S, Reddy V, McKay D. Crystal and solution structures of an HslUV protease-chaperone complex. Cell. 2000;103:633-43 pubmed
HslUV is a "prokaryotic proteasome" composed of the HslV protease and the HslU ATPase, a chaperone of the Clp/Hsp100 family. The 3.4 A crystal structure of an HslUV complex is presented here...
Trame C, McKay D. Structure of Haemophilus influenzae HslU protein in crystals with one-dimensional disorder twinning. Acta Crystallogr D Biol Crystallogr. 2001;57:1079-90 pubmed
The structure of the Haemophilus influenzae HslU protein, a molecular chaperone of the Clp/Hsp100 family, has been solved to 2.3 A by molecular replacement using a model of the homologous Escherichia coli protein...