1HT2

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

Summary for 1HT2

Entry DOI	10.2210/pdb1ht2/pdb
Related	1DOO 1E94 1HQY 1HT1
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 Cited by 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 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.8 Å)

Structure validation