1HT1

Nucleotide-Dependent Conformational Changes in a Protease-Associated ATPase HslU

Summary for 1HT1

• Entry DOI: 10.2210/pdb1ht1/pdb
• Related: 1DOO 1E94 1HQY 1HT2
• Descriptor: HEAT SHOCK LOCUS HSLV, HEAT SHOCK LOCUS HSLU, ADENOSINE-5'-DIPHOSPHATE (3 entities in total)
• Functional Keywords: hslvu, peptidase-atpase complex, chaperone
• Biological source: Escherichia coli; More
• Cellular location: Cytoplasm: P0A7B8 P0A6H5
• Total number of polymer chains: 12
• Total formula weight: 355584.06

Authors

Wang, J.,Song, J.J.,Seong, I.S.,Franklin, M.C.,Kamtekar, S.,Eom, S.H.,Chung, C.H. (deposition date: 2000-12-27, release date: 2001-11-14, Last modification date: 2024-02-07)

Primary citation

Wang, J.,Song, J.J.,Seong, I.S.,Franklin, M.C.,Kamtekar, S.,Eom, S.H.,Chung, C.H.
Nucleotide-dependent conformational changes in a protease-associated ATPase HsIU.
Structure, 9:1107-1116, 2001

PubMed Abstract: The bacterial heat shock locus ATPase HslU is an AAA(+) protein that has structures known in many nucleotide-free and -bound states. Nucleotide is required for the formation of the biologically active HslU hexameric assembly. The hexameric HslU ATPase binds the dodecameric HslV peptidase and forms an ATP-dependent HslVU protease.

PubMed: 11709174
DOI: 10.1016/S0969-2126(01)00670-0

Experimental method

X-RAY DIFFRACTION (2.8 Å)