Abstract
HslUV is a 'prokaryotic proteasome' composed of the HslV protease and the HslU ATPase, a chaperone of the Clp/Hsp100 family. The 3.4 Å crystal structure of an HslUV complex is presented here. Two hexameric ATP binding rings of HslU bind intimately to opposite sides of the HslV protease; the HslU 'intermediate domains' extend outward from the complex. The solution structure of HslUV, derived from small angle X-ray scattering data under conditions where the complex is assembled and active, agrees with this crystallographic structure. When the complex forms, the carboxy-terminan helices of HslU distend and bind between subunits of HslV, and the apical helices of HslV shift substantially, transmitting a conformational change to the active site region of the protease.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 633-643 |
| Number of pages | 11 |
| Journal | Cell |
| Volume | 103 |
| Issue number | 4 |
| DOIs | |
| State | Published - 2000 |
| Externally published | Yes |
Bibliographical note
Funding Information:We thank Lushen Li for excellent technical assistance in biochemistry, members of the SSRL and ALS staff for excellent beamline assistance, and Dimitri Svergun for helpful discussion on solution scattering analysis and the use of his programs Gnom, Crysol, and Crydam. This work was supported by award GM-39928 from the National Institutes of Health (NIH) to D. B. M.; V. R. is supported by the MMTSB research resource RR12255 of NIH to TSRI. This work is based upon research conducted at the Stanford Synchrotron Radiation Laboratory (SSRL), which is funded by the Department of Energy (BES, BER) and the National Institutes of Health (NCRR, NIGMS), and at the Advanced Light Source (ALS), which is funded by the Department of Energy.