1HJO

ATPase domain of human heat shock 70kDa protein 1

Summary for 1HJO

• Entry DOI: 10.2210/pdb1hjo/pdb
• Descriptor: PROTEIN (HEAT-SHOCK 70KD PROTEIN), CALCIUM ION, CHLORIDE ION, ... (5 entities in total)
• Functional Keywords: atp-binding, chaperone, heat shock, hydrolase
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm: P08107
• Total number of polymer chains: 1
• Total formula weight: 42385.12

Authors

Osipiuk, J.,Walsh, M.A.,Freeman, B.C.,Morimoto, R.I.,Joachimiak, A. (deposition date: 1998-10-13, release date: 1998-10-21, Last modification date: 2024-02-07)

Primary citation

Osipiuk, J.,Walsh, M.A.,Freeman, B.C.,Morimoto, R.I.,Joachimiak, A.
Structure of a new crystal form of human Hsp70 ATPase domain.
Acta Crystallogr.,Sect.D, 55:1105-1107, 1999

PubMed Abstract: Hsp70 proteins are highly conserved proteins induced by heat shock and other stress conditions. An ATP-binding domain of human Hsp70 protein has been crystallized in two major morphological forms at pH 7.0 in the presence of PEG 8000 and CaCl2. Both crystal forms belong to the orthorhombic space group P212121, but show no resemblance in unit-cell parameters. Analysis of the crystal structures for both forms shows a 1-2 A shift of one of the subdomains of the protein. This conformational change could reflect a 'natural' flexibility of the protein which might be relevant to ATP binding and may facilitate the interaction of other proteins with Hsp70 protein.

PubMed: 10216320
DOI: 10.1107/S0907444999002103

Experimental method

X-RAY DIFFRACTION (2.3 Å)