1G3I

CRYSTAL STRUCTURE OF THE HSLUV PROTEASE-CHAPERONE COMPLEX

Summary for 1G3I

• Entry DOI: 10.2210/pdb1g3i/pdb
• Related: 1G3K
• Descriptor: ATP-DEPENDENT HSLU PROTEASE ATP-BINDING SUBUNIT HSLU, ATP-DEPENDENT PROTEASE HSLV, ADENOSINE-5'-TRIPHOSPHATE (3 entities in total)
• Functional Keywords: chaperone/hydrolase, chaperone-hydrolase complex
• Biological source: Haemophilus influenzae; More
• Cellular location: Cytoplasm (By similarity): P43773 P43772
• Total number of polymer chains: 24
• Total formula weight: 826226.81

Authors

Sousa, M.C.,Trame, C.B.,Tsuruta, H.,Wilbanks, S.M.,Reddy, V.S.,McKay, D.B. (deposition date: 2000-10-24, release date: 2000-11-22, Last modification date: 2024-04-03)

Primary citation

Sousa, M.C.,Trame, C.B.,Tsuruta, H.,Wilbanks, S.M.,Reddy, V.S.,McKay, D.B.
Crystal and solution structures of an HslUV protease-chaperone complex.
Cell(Cambridge,Mass.), 103:633-643, 2000

PubMed 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 A 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-terminal 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.

PubMed: 11106733
DOI: 10.1016/S0092-8674(00)00166-5

Experimental method

X-RAY DIFFRACTION (3.41 Å)