HslUV is a "prokaryotic proteasome" made up of a double-donut protease (HslV) capped by two hexameric chaperone rings (HslU). HslU is a member of the Clp\Hsp100 chaperone family.

HslUV complex

Comparison of the structures of the HslU and HslV protomers in the HslUV complex to their uncomplexed structures reveals the conformational changes that take place when the complex forms and suggests a mechanism of activation of the HslV protease by the HslU chaperone.


Sousa, M. C., Trame, C. B., Tsuruta, H., Wilbanks, S. M., Reddy, V. S., and McKay, D. B.
"Crystal and Solution Structures of an HslUV Protease-Chaperone Complex."
Cell 103, 633-643 (2000).
[PubMed] [HslUV coordinates]

Trame, C. B. and McKay, D. B.
"Structure of Haemophilus influenzae HslU protein in crystals with one-dimensional disorder twinning."
Acta Crystallogr. D57, 1079-1090 (2001).
[PubMed] [HslU coordinates]

M. C. Sousa and McKay, D. B.
"Structure of Haemophilus influenzae HslV protein at 1.9 Angstrom resolution, revealing a cation binding site near the catalytic site"
Acta Cryst. D57, 1950-1954 (2001).
[PubMed] [HslV coordinates]

M. C. Sousa, B. M. Kessler, H. S. Overkleeft & D. B. McKay.
"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. 318, 779-785 (2002).
[PubMed] [HslUV NLVS coordinates]

A. R. Kwon, B. M. Kessler, H. S. Overkleeft & D. B. McKay.
"Structure and reactivity of an asymmetric complex between HslV and I-domain deleted HslU, a prokaryotic homolog of the eukaryotic proteasome"
J. Mol. Biol. 330, 185-195 (2003).
[PubMed] [HslU(delI)V native coordinates][HslU(delI)V NLVS coordinates]

A. R. Kwon, C. B. Trame & D. B. McKay.
"Kinetics of protein substrate degradation by HslUV"
J. Struct. Biol. 146 141-147 (2004).

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